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The antibody was purified by protein-G affinity chromatography, and conjugated with biotin under optimal conditions. The solution is free of unconjugated biotin.
Concentration:
0.5 mg/ml
Storage & Handling:
The antibody solution should be stored undiluted at 4°C. Do not freeze.
Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 5 μg antibody per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
COA:
Enter Lot#:
Jurkat cell extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with Biotin anti-Caspase 3 antibody (clone 4-1-18). Proteins were visualized using an HRP-conjugated Streptavidin and chemiluminescence detection.
Caspase 3 (also known as cpp32, Apopain, Yama, and PARP cleavage protease) is a member of the peptidase family C14. This cytoplasmic caspase functions as a heterotetramer and has two isoforms (one acts as a dominant negative inhibitor). The pro-form of this caspase is approximately 32 kD. Caspase 3 is involved in the caspase activation cascade responsible for apoptosis execution. This caspase cleaves/activates SREBPs, Caspase 6, Caspase 7, and Caspase 9. Caspase 3 is inhibited by c-IAP1, c-IAP2, XIAP, survivin, and Livin and activated by Caspase 6, -8 , and -10, granzyme B, Apaf-1 by cleavage into large p17 and small p12 subunits. Active heterodimers form between the large p17 subunit and small p11 subunit of Caspase 7 and vice versa. Caspase 3 has been shown to cleave PARP, huntingtin, androgen receptor, atrophin-1, DNA- PKcs, D4-GDI, hnRNPs C1/C2, U1snRNP, PKC delta, ATM, fodrin, gelsolin, ICAD, RIP, X-IAP, STAT1, topoisomerase I, vimentin, Rb, lamin B, mdm2, and β-catenin. The 4-1-18 monoclonal antibody has been shown to be useful for Western blotting of human caspase 3 (32 kD pro-caspase and 17 kD cleaved caspase).
Peptidase family C14, heterotetramer. Two isoforms, pro-Casp3 32 kD
Distribution:
Cytoplasm
Function:
Involved in caspase activation cascade responsible for apoptosis execution. Cleaves/activates SREBPs, Casp6, Casp7, Casp9
Regulation:
Inhibited by dominant negative isoform, c-IAP1, c-IAP2, XIAP, survivin, Livin. Activated when cleaved by Casp6, -8, -10, granzyme B, Apaf-1 into large p17 and small p12 subunits
Interaction:
Active heterodimers between large p17 subunit and small p11 subunit of Casp7 and vice versa. Cleaves PARP, huntingtin, androgen receptor, atrophin-1, DNA- PKcs, D4-GDI, hnRNPs C1/C2, U1snRNP, PKC delta, ATM, fodrin, gelsolin, ICAD, RIP, X-IAP, STAT1, topo
Antigen References:
1. Goldberg Y, et al. 1996. Nat. Genet. 13:442. 2. Fernandes-Alnemri T, et al. 1996. P. Natl. Acad. Sci. USA 93:7464. 3. Slee E, et al. 2001. J. Biol. Chem. 276:7320. 4. Woo M, et al. 2003. Nat. Immunol. 4:1016.
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This data display is provided for general comparisons between formats. Your actual data may vary due to variations in samples, target cells, instruments and their settings, staining conditions, and other factors. If you need assistance with selecting the best format contact our expert technical support team.
Biotin anti-Caspase-3
Jurkat cell extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with Biotin anti-Caspase 3 antibody (clone 4-1-18). Proteins were visualized using an HRP-conjugated Streptavidin and chemiluminescence detection.
Purified anti-Caspase-3
Jurkat cell extract was resolved by electrophoresis, transferred to nitrocellulose, and probed with mouse anti-caspase 3 (clone 4-1-18). Proteins were visualized using a goat anti-mouse secondary conjugated to HRP and a chemiluminescence detection system.