Anti-Cleaved-Caspase-3 p17 (D175) antibody

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Product name Anti-Cleaved-Caspase-3 p17 (D175) antibody
Short Description Rabbit polyclonal against Cleaved-Caspase-3 p17 (D175)
Description Rabbit polyclonal to Cleaved-Caspase-3 p17 (D175).
Applications ELISA, IHC-p
Dilution range IHC 1:100-1:300
ELISA 1:20000
Specificity Cleaved-Caspase-3 p17 (D175) polyclonal antibody detects endogenous levels of fragment of activated Caspase-3 p17 protein resulting from cleavage adjacent to D175.
Protein Name Caspase-3
Cysteine Protease Cpp32
Protein Yama
Srebp Cleavage Activity 1
Sca-1 [Cleaved Into-Caspase-3 Subunit P17-Caspase-3 Subunit P12]
Immunogen Synthesized peptide derived from human Caspase-3 p17
Immunogen Region 110-190 aa, Internal
Storage Instruction Store at-20°C, and avoid repeat freeze-thaw cycles.
Host Rabbit
Clonality Polyclonal
Reactivity Human
Conjugation Unconjugated
Concentration 1 mg/ml
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Isotype IgG
Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Gene ID 836
Gene Symbol CASP3
Molecular Weight 17 kDa
Database Links HGNC:1504
Alternative Names Anti-Caspase-3 antibody
Anti-Casp-3 antibody
Anti-Apopain antibody
Anti-Cysteine Protease Cpp32 antibody
Anti-Cpp-32 antibody
Anti-Protein Yama antibody
Anti-Srebp Cleavage Activity 1 antibody
Anti-Sca-1 [Cleaved Into-Caspase-3 Subunit P17-Caspase-3 Subunit P12] antibody
Anti-CASP3 CPP32 antibody
Function Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and-9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.
Post-translational Modifications Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.; S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol.
Cellular Localization Cytoplasm
Tissue Specificity Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.
Swiss-Prot Key CASP3_HUMAN
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