Zfp57 inactivation illustrates the role of ICR methylation in imprinted gene expression during neural differentiation of mouse ESCs

Zfp57 inactivation illustrates the role of ICR methylation in imprinted gene expression during neural differentiation of mouse ESCs
ZFP57 is required to keep up the germline-marked differential methylation at imprinting management areas (ICRs) in mouse embryonic stem cells (ESCs). Although DNA methylation has a key role in genomic imprinting, a number of imprinted genes are managed by completely different mechanisms, and a complete research of the relationship between DMR methylation and imprinted gene expression is missing. To tackle the latter subject, we differentiated wild-type and Zfp57-/- hybrid mouse ESCs into neural precursor cells (NPCs) and evaluated allelic expression of imprinted genes.
In mutant NPCs, we noticed a discount of allelic bias of all the 32 genes that had been imprinted in wild-type cells, demonstrating that ZFP57-dependent methylation is required for sustaining or buying imprinted gene expression during differentiation. Analysis of expression ranges confirmed that imprinted genes expressed from the non-methylated chromosome had been usually up-regulated, and people expressed from the methylated chromosome had been down-regulated in mutant cells.
However, expression ranges of a number of imprinted genes buying biallelic expression weren’t affected, suggesting the existence of compensatory mechanisms that management their RNA stage. Since neural differentiation was partially impaired in Zfp57-mutant cells, this research additionally signifies that imprinted genes and/or non-imprinted ZFP57-target genes are required for correct neurogenesis in cultured ESCs.

Expression of cardiac copper chaperone encoding genes and their correlation with cardiac operate parameters in goats

Copper deficiency (CuD) is a typical trigger of oxidative cardiac tissue harm in ruminants. The expression of copper chaperone (Cu-Ch) encoding genes permits an in-depth understanding of copper-associated problems, however no earlier research have been undertaken to spotlight Cu-Ch disturbances in coronary heart tissue in ruminants as a result of CuD. The present research aimed to research the Cu-Ch mRNA expression in the coronary heart of goats after experimental CuD and spotlight their relationship with the cardiac measurements.
Eleven male goats had been enrolled in this research and divided into the management group (n = 4) and CuD group (n = 7), which obtained copper-reducing dietary regimes for 7 months. Heart operate was evaluated by electrocardiography and echocardiography, and at the finish of the experiment, all animals had been sacrificed and the cardiac tissues had been collected for histopathology and quantitative mRNA expression by real-time PCR.
In the therapy group, cardiac measurements revealed elevated preload and the existence of cardiac dilatation, and vital cardiac tissue harm by histopathology. Also, the relative mRNA expression of Cu-Ch encoding genes; ATP7A, CTr1, LOX, COX17, in addition to ceruloplasmin (CP), troponin I3 (TNNI3), glutathione peroxidase (GPX1), and matrix metalloprotease inhibitor (MMPI1) genes had been considerably down-regulated in CuD group.
There was a major correlation between investigated genes and a few cardiac operate measurements; in the meantime, a major inverse correlation was noticed between histopathological rating and ATP7B, CTr1, LOX, and COX17. In conclusion, this research revealed that CuD induces cardiac dilatation and alters the mRNA expression of Cu-Ch genes, in addition to TNNI3, GPX1, and MMPI1 which are thought of key components in clinically undetectable CuD-induced cardiac harm in goats which necessitate additional research for feasibility as biomarkers.

Transcriptome and Degradome Profiling Reveals a Role of miR530 in the Circadian Regulation of Gene Expression in Kalanchoë marnieriana

Crassulacean acid metabolism (CAM) is a vital photosynthetic pathway for plant adaptation to dry environments. CAM crops characteristic a coordinated interplay between mesophyll and dermis features that includes refined laws of gene expression. Plant microRNAs (miRNAs) are essential post-transcription regulators of gene expression, nonetheless, their roles underlying the CAM pathway stay poorly investigated. Here, we current a research characterizing the expression of miRNAs in an obligate CAM species Kalanchoë marnieriana.
Through sequencing of transcriptome and degradome in mesophyll and epidermal tissues underneath the drought remedies, we recognized differentially expressed miRNAs that had been probably concerned in the regulation of CAM. In whole, we obtained 84 miRNA genes, and eight of them had been decided to be Kalanchoë-specific miRNAs. It is broadly accepted that CAM pathway is regulated by circadian clock.
We confirmed that miR530 was considerably downregulated in epidermal peels underneath drought situations; miR530 focused two tandem zinc knuckle/PLU3 area encoding genes (TZPs) that had been probably concerned in mild signaling and circadian clock pathways. Our work means that the miR530-TZPs module would possibly play a role of regulating CAM-related gene expression in Kalanchoë.
Zfp57 inactivation illustrates the role of ICR methylation in imprinted gene expression during neural differentiation of mouse ESCs

Integrative Modelling of Gene Expression and Digital Phenotypes to Describe Senescence in Wheat

Senescence is the ultimate stage of leaf growth and is important for crops’ health as nutrient relocation from leaves to reproductive organs takes place. Although senescence is vital in nutrient relocation and yield dedication in cereal grain manufacturing, there may be restricted understanding of the genetic and molecular mechanisms that management it in main staple crops equivalent to wheat. Senescence is a extremely orchestrated continuum of interacting pathways all through the lifecycle of a plant. Levels of gene expression, morphogenesis, and phenotypic growth all play key roles.
Yet, most research give attention to a brief window instantly after anthesis. This strategy clearly leaves out key elements controlling the activation, growth, and modulation of the senescence pathway earlier than anthesis, in addition to during the later developmental phases, during which grain growth continues. Here, a computational multiscale modelling strategy integrates multi-omics developmental knowledge to try to simulate senescence at the molecular and plant stage.
To recreate the senescence course of in wheat, core rules had been borrowed from Arabidopsis Thaliana, a extra broadly researched plant mannequin. The resulted mannequin describes temporal gene regulatory networks and their impact on plant morphology resulting in senescence. Digital phenotypes generated from photos utilizing a phenomics platform had been used to seize the dynamics of plant growth.

EP Reagent Biuret Reagent

1011601 1L
EUR 42.18

EP Reagent Iodoplatinate Reagent

1046300 200ML
EUR 360.24

EP Reagent Methoxyphenylacetic Reagent

1053601 100ML
EUR 354.54

EP Reagent Molybdovanadic Reagent

1056700 100ML
EUR 42.18

EP Reagent Phosphomolybdotungstic Reagent

1065000 100ML
EUR 161.88

Automatic CO2 Change Over Unit

INC6176 EACH
EUR 1288.2

Forceps Dissecting Turn Over End

D02129 EACH
EUR 4.67

Gas Change Over Unit 30Psi

GAS1000 EACH
EUR 904.02

Gas Change Over Unit 60Psi

GAS1002 EACH
EUR 905.16

Gas Change Over Unit 100Psi

GAS1004 EACH
EUR 922.26

Bolle TG10 Safety Over Glasses

SAF1106 EACH
EUR 8.39

BMP3 antibody

70R-12376 100 ug
EUR 523.2
Description: Rabbit polyclonal BMP3 antibody

BMP3 antibody

70R-12406 100 ug
EUR 536.4
Description: Goat polyclonal BMP3 antibody

BMP3 antibody

70R-12407 100 ug
EUR 523.2
Description: Rabbit polyclonal BMP3 antibody

BMP3 antibody

70R-49417 100 ul
EUR 292.8
Description: Purified Polyclonal BMP3 antibody

BMP3 antibody

70R-35783 100 ug
EUR 392.4
Description: Rabbit polyclonal BMP3 antibody

BMP3 Peptide

46-818P 0.1 mg
EUR 405.6
Description: BMP3 Peptide

BMP3 protein

30R-2364 50 ug
EUR 403.2
Description: Purified recombinant Human BMP3 protein

BMP3 Antibody

35653-100ul 100ul
EUR 302.4

BMP3 Antibody

34500-100ul 100ul
EUR 302.4

BMP3 Antibody

34500-50ul 50ul
EUR 224.4

BMP3 Antibody

ABF5153 100 ug
EUR 525.6

BMP3 Antibody

ABD3848 100 ug
EUR 525.6

BMP3 siRNA

20-abx900650
  • EUR 661.20
  • EUR 878.40
  • 15 nmol
  • 30 nmol

BMP3 siRNA

20-abx909172
  • EUR 661.20
  • EUR 878.40
  • 15 nmol
  • 30 nmol

BMP3 siRNA

20-abx909173
  • EUR 661.20
  • EUR 878.40
  • 15 nmol
  • 30 nmol

BMP3 Antibody

1-CSB-PA001003
  • EUR 266.40
  • EUR 234.00
  • 100ug
  • 50ug
Description: A polyclonal antibody against BMP3. Recognizes BMP3 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: WB, IHC, ELISA;WB:1/500-1/2000.IHC:1/100-1/300.ELISA:1/40000

BMP3 Antibody

1-CSB-PA001013
  • EUR 266.40
  • EUR 234.00
  • 100ug
  • 50ug
Description: A polyclonal antibody against BMP3. Recognizes BMP3 from Human. This antibody is Unconjugated. Tested in the following application: WB, ELISA;WB:1/500-1/2000.ELISA:1/5000

BMP3 Antibody

1-CSB-PA901137
  • EUR 380.40
  • EUR 292.80
  • 100ul
  • 50ul
Description: A polyclonal antibody against BMP3. Recognizes BMP3 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC;ELISA:1:1000-1:2000, WB:1:200-1:1000, IHC:1:25-1:100

BMP3 Antibody

1-CSB-PA930762
  • EUR 380.40
  • EUR 292.80
  • 100ul
  • 50ul
Description: A polyclonal antibody against BMP3. Recognizes BMP3 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: ELISA, IHC;ELISA:1:1000-1:2000, IHC:1:15-1:50

BMP3 Antibody

DF3848 200ul
EUR 420

BMP3 Antibody

AF5153 200ul
EUR 420

BMP3 Antibody

1-CSB-PA192641
  • EUR 380.40
  • EUR 292.80
  • 100ul
  • 50ul
Description: A polyclonal antibody against BMP3. Recognizes BMP3 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, IHC;ELISA:1:1000-1:2000, IHC:1:25-1:100

BMP3 Antibody

CSB-PA105888-
EUR 402
Description: A polyclonal antibody against BMP3. Recognizes BMP3 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB;WB:1:500-1:3000

BMP3 Antibody

CSB-PA105888-100ul 100ul
EUR 379.2
Description: A polyclonal antibody against BMP3. Recognizes BMP3 from Human. This antibody is Unconjugated. Tested in the following application: ELISA, WB;WB:1:500-1:3000

BMP3 Antibody

1-CSB-PA005413
  • EUR 266.40
  • EUR 234.00
  • 100ug
  • 50ug
Description: A polyclonal antibody against BMP3. Recognizes BMP3 from Human, Mouse, Rat. This antibody is Unconjugated. Tested in the following application: WB, ELISA;WB:1/500-1/2000.ELISA:1/20000

BMP3 Antibody

1-CSB-PA002739LA01HU
  • EUR 380.40
  • EUR 402.00
  • 100ug
  • 50ug
Description: A polyclonal antibody against BMP3. Recognizes BMP3 from Human, Mouse. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC; Recommended dilution: WB:1:1000-1:5000, IHC:1:20-1:200

anti-BMP3

YF-PA23307 50 ul
EUR 400.8
Description: Mouse polyclonal to BMP3

anti-BMP3

YF-PA10496 50 ul
EUR 435.6
Description: Mouse polyclonal to BMP3

BMP3 Antibody

F45244-0.08ML 0.08 ml
EUR 165

BMP3 Antibody

F45244-0.4ML 0.4 ml
EUR 379

BMP3 Antibody

F45376-0.08ML 0.08 ml
EUR 165

BMP3 Antibody

F45376-0.4ML 0.4 ml
EUR 379

EP Reagent Sulfomolybdic Reagent R3

1086500 1L
EUR 287.28

DURAN Over-Cap 45mm Black Phenolic

BOT2596 PK10
EUR 25.08

BMP3 Blocking Peptide

33R-11055 50 ug
EUR 229.2
Description: A synthetic peptide for use as a blocking control in assays to test for specificity of BMP3 antibody, catalog no. 70R-12407

BMP3 Blocking Peptide

20-abx062292
  • EUR 326.40
  • EUR 493.20
  • 1 mg
  • 5 mg

BMP3 Rabbit pAb

A6877-100ul 100 ul
EUR 369.6

BMP3 Rabbit pAb

A6877-200ul 200 ul
EUR 550.8

BMP3 Rabbit pAb

A6877-20ul 20 ul
EUR 219.6

BMP3 Rabbit pAb

A6877-50ul 50 ul
EUR 267.6

BMP3 Blocking Peptide

DF3848-BP 1mg
EUR 234

BMP3 Conjugated Antibody

C35653 100ul
EUR 476.4

BMP3 Blocking Peptide

AF5153-BP 1mg
EUR 234

BMP3 cloning plasmid

CSB-CL002739HU-10ug 10ug
EUR 279.6
Description: A cloning plasmid for the BMP3 gene.

Anti-BMP3 antibody

PAab00918 100 ug
EUR 426

anti- BMP3 antibody

FNab00918 100µg
EUR 606.3
Description: Antibody raised against BMP3

Anti-BMP3 antibody

STJ28957 100 µl
EUR 332.4
Description: BMP3 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein, also known as osteogenin, induces bone formation.

Anti-BMP3 antibody

STJ71562 100 µg
EUR 312

BMP3 Polyclonal Antibody

A52753
  • EUR 684.66
  • Ask for price
  • Ask for price
  • EUR 423.50
  • 100 µg
  • 20 ul
  • 50 ul
  • 100 ul

BMP3 Polyclonal Antibody

A71005
  • EUR 302.50
  • EUR 423.50
  • 50 ul
  • 100 ul

BMP3 Polyclonal Antibody

A52753-020 20 ul Ask for price

BMP3 Polyclonal Antibody

A52753-050 50 ul Ask for price

BMP3 Polyclonal Antibody

A52753-100 100 ul
EUR 423.5

BMP3 Polyclonal Antibody

A71005-050 50 ul
EUR 302.5

BMP3 Polyclonal Antibody

A71005-100 100 ul
EUR 423.5

BOP reagent

5-02141 25g Ask for price

BOP reagent

5-02142 100g Ask for price

Chymase reagent

30C-CP1129 5 units
EUR 2622
Description: Purified native Human Chymase reagent

Traut's Reagent

2330-1000
EUR 418.8

Traut's Reagent

2330-500
EUR 248.4

MTS Reagent

2808-1000
EUR 1188

MTS Reagent

2808-250
EUR 438

MTT Reagent

2809-1G
EUR 216

MTT Reagent

2809-5G
EUR 652.8

BOP reagent

A7015-100000 100 g
EUR 240
Description: A peptide coupling reagent. Can be used in the preparation of phenyl esters of amino acids which have been shown to be valuable as blocked derivatives of amino acids in the field of peptide synthesis.

BOP reagent

A7015-25000 25 g
EUR 135.6
Description: A peptide coupling reagent. Can be used in the preparation of phenyl esters of amino acids which have been shown to be valuable as blocked derivatives of amino acids in the field of peptide synthesis.

Bradford reagent

BDE641 100ml
EUR 73.21

Bluing Reagent

BRT030 30 ml
EUR 72

Bluing Reagent

BRT125 125 ml
EUR 75.6

Bluing Reagent

BRT3800 1 Gal.
EUR 220.8

Bluing Reagent

BRT500 500 ml
EUR 91.2

Bluing Reagent

BRT999 1000 ml
EUR 105.6

Beaucage reagent

HY-100951 10mM/1mL
EUR 151.2

Phosphate Reagent

106199 PK100
EUR 61.29

Chromium Reagent

1206699 EACH
EUR 141.72

Ninhydrin Reagent

MIC6746 EACH
EUR 31.12

Nessler Reagent

NESSR 500ML
EUR 148.2

Thioacetamide Reagent

THIOR01 100ML
EUR 78.66

HEK-293T Telomerase Over-Expressing Cell Pellet

abx069991-1Pellet 1 Pellet
EUR 477.6

Visitor Eye Shield Over Specs - Portwest PW30

SAF1021 EACH
EUR 3.42

Esophagus Lysate

1365 0.1 mg
EUR 229.2
Description: Esophagus tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Ileum Lysate

1367 0.1 mg
EUR 229.2
Description: Ileum tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Rectum Lysate

1373 0.1 mg
EUR 229.2
Description: Rectum tissue lysate was prepared by homogenization in homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Skin Lysate

1376 0.1 mg
EUR 229.2
Description: Skin tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Thyroid Lysate

1380 0.1 mg
EUR 229.2
Description: Thyroid tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Spleen Lysate

1406 0.1 mg
EUR 229.2
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Bladder Lysate

1410 0.1 mg
EUR 229.2
Description: Bladder tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Cerebellum Lysate

1412 0.1 mg
EUR 229.2
Description: Cerebellum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Cerebrum Lysate

1413 0.1 mg
EUR 229.2
Description: Cerebrum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Pancreas Lysate

1414 0.1 mg
EUR 229.2
Description: Pancreas tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Stomach Lysate

1415 0.1 mg
EUR 229.2
Description: Stomach tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Testis Lysate

1416 0.1 mg
EUR 229.2
Description: Testis tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Adrenal Lysate

1417 0.1 mg
EUR 229.2
Description: Adrenal tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Skin Lysate

1419 0.1 mg
EUR 229.2
Description: Skin tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Eye Lysate

1420 0.1 mg
EUR 229.2
Description: Eye tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Trachea Lysate

1422 0.1 mg
EUR 229.2
Description: Trachea tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Lung Lysate

1462 0.1 mg
EUR 229.2
Description: Lung tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Liver Lysate

1464 0.1 mg
EUR 229.2
Description: Liver tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Kidney Lysate

1465 0.1 mg
EUR 229.2
Description: Kidney tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Spleen Lysate

1466 0.1 mg
EUR 229.2
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

L1210 Lysate

1284 0.1 mg
EUR 229.2
Description: L1210 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The L1210 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

C2C12 Lysate

1285 0.1 mg
EUR 229.2
Description: C2C12 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The C2C12 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

P815 Lysate

1286 0.1 mg
EUR 229.2
Description: P815 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The P815 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

EL4 Lysate

1287 0.1 mg
EUR 229.2
Description: EL4 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The EL4 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Lung Lysate

1302 0.1 mg
EUR 229.2
Description: Lung tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Spleen Lysate

1306 0.1 mg
EUR 229.2
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Placenta Lysate

1309 0.1 mg
EUR 229.2
Description: Placenta tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Melanoma Lysate

20-101 0.1 mg
EUR 632.4
Description: Melanoma lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human melanoma tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the melanoma tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The melanoma tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Trachea Lysate

20-102 0.1 mg
EUR 500.1
Description: Human trachea lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The human trachea tissue total protein is provided in a buffer including HEPES (pH7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the trachea tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The trachea tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Jurkat Lysate

1205 0.1 mg
EUR 229.2
Description: Jurkat lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The Jurkat lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

MOLT4 Lysate

1206 0.1 mg
EUR 229.2
Description: MOLT4 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The MOLT4 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

HL60 Lysate

1209 0.1 mg
EUR 229.2
Description: HL60 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The HL60 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

T24 Lysate

1213 0.1 mg
EUR 229.2
Description: T24 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The T24 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

U937 Lysate

1215 0.1 mg
EUR 229.2
Description: U937 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The U937 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

MCF7 Lysate

1219 0.1 mg
EUR 229.2
Description: MCF7 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The MCF7 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Ramos Lysate

1225 0.1 mg
EUR 229.2
Description: Ramos lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The Ramos lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT.

Kidney Lysate

21-104 0.1 mg
EUR 342.6
Description: Bovine kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The bovine kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Liver Lysate

21-105 0.1 mg
EUR 342.6
Description: Bovine liver tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The bovine liver tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the liver tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The liver tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Heart Lysate

21-115 0.1 mg
EUR 342.6
Description: Guinea Pig heart tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The guinea pig heart tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the heart tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The heart tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Kidney Lysate

21-116 0.1 mg
EUR 342.6
Description: Guinea Pig kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The guinea pig kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Adrenal Lysate

21-160 0.1 mg
EUR 468.6
Description: Monkey (Cynomolgus) adrenal tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) adrenal tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the adrenal tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The adrenal tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Colon Lysate

21-179 0.1 mg
EUR 342.6
Description: Monkey (Cynomolgus) colon tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) colon tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the colon tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The colon tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Gallbladder Lysate

21-188 0.1 mg
EUR 468.6
Description: Monkey (Cynomolgus) gallbladder tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) gallbladder tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the gallbladder tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The gallbladder tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Kidney Lysate

21-190 0.1 mg
EUR 342.6
Description: Monkey (Cynomolgus) kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Lung Lysate

21-194 0.1 mg
EUR 342.6
Description: Monkey (Cynomolgus) lung tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) lung tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the lung tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The lung tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Skin Lysate

21-204 0.1 mg
EUR 468.6
Description: Monkey (Cynomolgus) skin tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) skin tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the skin tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The skin tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Spleen Lysate

21-209 0.1 mg
EUR 342.6
Description: Monkey (Cynomolgus) spleen tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) spleen tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the spleen tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The spleen tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Brain Lysate

21-272 0.1 mg
EUR 342.6
Description: Monkey (Rhesus) brain tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) brain tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the brain tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The brain tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Colon Lysate

21-288 0.1 mg
EUR 342.6
Description: Monkey (Rhesus) colon tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) colon tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the colon tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The colon tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Gallbladder Lysate

21-298 0.1 mg
EUR 468.6
Description: Monkey (Rhesus) gallbladder tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) gallbladder tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the gallbladder tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The gallbladder tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Heart Lysate

21-299 0.1 mg
EUR 468.6
Description: Monkey (Rhesus) heart tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) heart tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the heart tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The heart tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Lung Lysate

21-305 0.1 mg
EUR 342.6
Description: Monkey (Rhesus) lung tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) lung tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the lung tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The lung tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.

Skin Lysate

21-315 0.1 mg
EUR 468.6
Description: Monkey (Rhesus) skin tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) skin tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the skin tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The skin tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot.
This work offers the foundation for the utility of computational modelling to advance understanding of the advanced organic trait senescence. This helps the growth of a predictive framework enabling its prediction in altering or excessive environmental situations, with a view to focused choice for optimum lifecycle period for bettering resilience to local weather change.

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