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.

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.

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	Scientific Laboratory Supplies	1L	EUR 42.18

EP Reagent Iodoplatinate Reagent
1046300	Scientific Laboratory Supplies	200ML	EUR 360.24

EP Reagent Methoxyphenylacetic Reagent
1053601	Scientific Laboratory Supplies	100ML	EUR 354.54

EP Reagent Molybdovanadic Reagent
1056700	Scientific Laboratory Supplies	100ML	EUR 42.18

EP Reagent Phosphomolybdotungstic Reagent
1065000	Scientific Laboratory Supplies	100ML	EUR 161.88

Automatic CO2 Change Over Unit
INC6176	Scientific Laboratory Supplies	EACH	EUR 1288.2

Forceps Dissecting Turn Over End
D02129	Scientific Laboratory Supplies	EACH	EUR 4.67

Gas Change Over Unit 30Psi
GAS1000	Scientific Laboratory Supplies	EACH	EUR 904.02

Gas Change Over Unit 60Psi
GAS1002	Scientific Laboratory Supplies	EACH	EUR 905.16

Gas Change Over Unit 100Psi
GAS1004	Scientific Laboratory Supplies	EACH	EUR 922.26

Bolle TG10 Safety Over Glasses
SAF1106	Scientific Laboratory Supplies	EACH	EUR 8.39

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 Antibody
ABF5153	Lifescience Market	100 ug	EUR 525.6

BMP3 Antibody
ABD3848	Lifescience Market	100 ug	EUR 525.6

BMP3 siRNA
20-abx900650	Abbexa	EUR 661.20 EUR 878.40	15 nmol 30 nmol

BMP3 siRNA
20-abx909172	Abbexa	EUR 661.20 EUR 878.40	15 nmol 30 nmol

BMP3 siRNA
20-abx909173	Abbexa	EUR 661.20 EUR 878.40	15 nmol 30 nmol

BMP3 Antibody
1-CSB-PA001003	Cusabio	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	Cusabio	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	Cusabio	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	Cusabio	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	Affbiotech	200ul	EUR 420

BMP3 Antibody
AF5153	Affbiotech	200ul	EUR 420

BMP3 Antibody
1-CSB-PA192641	Cusabio	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-	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	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	Cusabio	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	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 Antibody
F45244-0.08ML	NSJ Bioreagents	0.08 ml	EUR 165

BMP3 Antibody
F45244-0.4ML	NSJ Bioreagents	0.4 ml	EUR 379

BMP3 Antibody
F45376-0.08ML	NSJ Bioreagents	0.08 ml	EUR 165

BMP3 Antibody
F45376-0.4ML	NSJ Bioreagents	0.4 ml	EUR 379

EP Reagent Sulfomolybdic Reagent R3
1086500	Scientific Laboratory Supplies	1L	EUR 287.28

DURAN Over-Cap 45mm Black Phenolic
BOT2596	Scientific Laboratory Supplies	PK10	EUR 25.08

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	EUR 326.40 EUR 493.20	1 mg 5 mg

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
PAab00918	Lifescience Market	100 ug	EUR 426

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.

Anti-BMP3 antibody
STJ71562	St John's Laboratory	100 µg	EUR 312

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
A71005	EpiGentek	EUR 302.50 EUR 423.50	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

BOP reagent
5-02141	CHI Scientific	25g	Ask for price

BOP reagent
5-02142	CHI Scientific	100g	Ask for price

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

Traut's Reagent
2330-1000	Biovision		EUR 418.8

Traut's Reagent
2330-500	Biovision		EUR 248.4

MTS Reagent
2808-1000	Biovision		EUR 1188

MTS Reagent
2808-250	Biovision		EUR 438

MTT Reagent
2809-1G	Biovision		EUR 216

MTT Reagent
2809-5G	Biovision		EUR 652.8

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

Bluing Reagent
BRT030	ScyTek Laboratories	30 ml	EUR 72

Bluing Reagent
BRT125	ScyTek Laboratories	125 ml	EUR 75.6

Bluing Reagent
BRT3800	ScyTek Laboratories	1 Gal.	EUR 220.8

Bluing Reagent
BRT500	ScyTek Laboratories	500 ml	EUR 91.2

Bluing Reagent
BRT999	ScyTek Laboratories	1000 ml	EUR 105.6

Beaucage reagent
HY-100951	MedChemExpress	10mM/1mL	EUR 151.2

Phosphate Reagent
106199	Scientific Laboratory Supplies	PK100	EUR 61.29

Chromium Reagent
1206699	Scientific Laboratory Supplies	EACH	EUR 141.72

Ninhydrin Reagent
MIC6746	Scientific Laboratory Supplies	EACH	EUR 31.12

Nessler Reagent
NESSR	Scientific Laboratory Supplies	500ML	EUR 148.2

Thioacetamide Reagent
THIOR01	Scientific Laboratory Supplies	100ML	EUR 78.66

HEK-293T Telomerase Over-Expressing Cell Pellet
abx069991-1Pellet	Abbexa	1 Pellet	EUR 477.6

Visitor Eye Shield Over Specs - Portwest PW30
SAF1021	Scientific Laboratory Supplies	EACH	EUR 3.42

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.