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.

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.
BMP3 antibody |
70R-12376 |
Fitzgerald |
100 ug |
EUR 523.2 |
Description: Rabbit polyclonal BMP3 antibody |
BMP3 antibody |
70R-12406 |
Fitzgerald |
100 ug |
EUR 536.4 |
Description: Goat polyclonal BMP3 antibody |
BMP3 antibody |
70R-12407 |
Fitzgerald |
100 ug |
EUR 523.2 |
Description: Rabbit polyclonal BMP3 antibody |
BMP3 antibody |
70R-49417 |
Fitzgerald |
100 ul |
EUR 292.8 |
Description: Purified Polyclonal BMP3 antibody |
BMP3 antibody |
70R-35783 |
Fitzgerald |
100 ug |
EUR 392.4 |
Description: Rabbit polyclonal BMP3 antibody |
BMP3 Peptide |
46-818P |
ProSci |
0.1 mg |
EUR 405.6 |
Description: BMP3 Peptide |
BMP3 protein |
30R-2364 |
Fitzgerald |
50 ug |
EUR 403.2 |
Description: Purified recombinant Human BMP3 protein |
BMP3 Antibody |
35653-100ul |
SAB |
100ul |
EUR 302.4 |
BMP3 Antibody |
34500-100ul |
SAB |
100ul |
EUR 302.4 |
BMP3 Antibody |
34500-50ul |
SAB |
50ul |
EUR 224.4 |
BMP3 siRNA |
20-abx900650 |
Abbexa |
|
|
|
BMP3 siRNA |
20-abx909172 |
Abbexa |
|
|
|
BMP3 siRNA |
20-abx909173 |
Abbexa |
|
|
|
BMP3 Antibody |
1-CSB-PA001003 |
Cusabio |
|
|
|
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 |
Cusabio |
|
|
|
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 |
Cusabio |
|
|
|
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 |
Cusabio |
|
|
|
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 |
1-CSB-PA192641 |
Cusabio |
|
|
|
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- |
Cusabio |
|
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 |
Cusabio |
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 |
Cusabio |
|
|
|
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 |
Cusabio |
|
|
|
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 |
Abfrontier |
50 ul |
EUR 400.8 |
Description: Mouse polyclonal to BMP3 |
anti-BMP3 |
YF-PA10496 |
Abfrontier |
50 ul |
EUR 435.6 |
Description: Mouse polyclonal to BMP3 |
BMP3 Blocking Peptide |
33R-11055 |
Fitzgerald |
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 |
Abbexa |
|
|
|
BMP3 Rabbit pAb |
A6877-100ul |
Abclonal |
100 ul |
EUR 369.6 |
BMP3 Rabbit pAb |
A6877-200ul |
Abclonal |
200 ul |
EUR 550.8 |
BMP3 Rabbit pAb |
A6877-20ul |
Abclonal |
20 ul |
EUR 219.6 |
BMP3 Rabbit pAb |
A6877-50ul |
Abclonal |
50 ul |
EUR 267.6 |
BMP3 Blocking Peptide |
DF3848-BP |
Affbiotech |
1mg |
EUR 234 |
BMP3 Conjugated Antibody |
C35653 |
SAB |
100ul |
EUR 476.4 |
BMP3 Blocking Peptide |
AF5153-BP |
Affbiotech |
1mg |
EUR 234 |
BMP3 cloning plasmid |
CSB-CL002739HU-10ug |
Cusabio |
10ug |
EUR 279.6 |
|
Description: A cloning plasmid for the BMP3 gene. |
anti- BMP3 antibody |
FNab00918 |
FN Test |
100µg |
EUR 606.3 |
|
Description: Antibody raised against BMP3 |
Anti-BMP3 antibody |
STJ28957 |
St John's Laboratory |
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. |
BMP3 Polyclonal Antibody |
A52753 |
EpiGentek |
-
EUR 684.66
-
Ask for price
-
Ask for price
-
EUR 423.50
|
- 100 µg
- 20 ul
- 50 ul
- 100 ul
|
BMP3 Polyclonal Antibody |
A52753-020 |
EpiGentek |
20 ul |
Ask for price |
BMP3 Polyclonal Antibody |
A52753-050 |
EpiGentek |
50 ul |
Ask for price |
BMP3 Polyclonal Antibody |
A52753-100 |
EpiGentek |
100 ul |
EUR 423.5 |
BMP3 Polyclonal Antibody |
A71005-050 |
EpiGentek |
50 ul |
EUR 302.5 |
BMP3 Polyclonal Antibody |
A71005-100 |
EpiGentek |
100 ul |
EUR 423.5 |
Chymase reagent |
30C-CP1129 |
Fitzgerald |
5 units |
EUR 2622 |
Description: Purified native Human Chymase reagent |
Traut's Reagent |
2330-1000 |
Biovision |
|
EUR 418.8 |
BOP reagent |
A7015-100000 |
ApexBio |
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 |
ApexBio |
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 |
Bio Basic |
100ml |
EUR 73.21 |
|
HEK-293T Telomerase Over-Expressing Cell Pellet |
abx069991-1Pellet |
Abbexa |
1 Pellet |
EUR 477.6 |
|
Esophagus Lysate |
1365 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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 |
ProSci |
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.