ARG66888

anti-Caspase 3 (cleaved) antibody

anti-Caspase 3 (cleaved) antibody for ICC/IF,IHC-Formalin-fixed paraffin-embedded sections,Western blot and Human,Mouse,Rat

publication_link Publication2

Overview

Product Description Mouse Monoclonal antibody recognizes Caspase 3 (cleaved)
Tested Reactivity Hu, Ms, Rat
Tested Application ICC/IF, IHC-P, WB
Host Mouse
Clonality Monoclonal
Isotype IgG
Target Name Caspase 3 (cleaved)
Antigen Species Human
Immunogen Recombinant protein of cleaved Caspase 3.
Conjugation Un-conjugated
Alternate Names CPP-32; Caspase-3; EC 3.4.22.56; Apopain; CASP-3; CPP32; Cysteine protease CPP32; SCA-1; SREBP cleavage activity 1; CPP32B; Protein Yama

Application Instructions

Application Suggestion
Tested Application Dilution
ICC/IF1:50 - 1:200
IHC-P1:100 - 1:200
WB1:250 - 1:1000
Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist.
Positive Control HeLa, NIH/3T3 and Rat brain
Observed Size ~ 20 kDa (cleaved form)

Properties

Form Liquid
Purification Affinity purification with immunogen.
Buffer PBS (pH 7.4), 0.02% Sodium azide, 50% Glycerol and 0.5% BSA.
Preservative 0.02% Sodium azide
Stabilizer 50% Glycerol and 0.5% BSA
Storage Instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use.
Note For laboratory research only, not for drug, diagnostic or other use.

Bioinformation

Database Links

GeneID: 12367 Mouse CASP3

GeneID: 25402 Rat CASP3

GeneID: 836 Human CASP3

Gene Symbol CASP3
Gene Full Name caspase 3, apoptosis-related cysteine peptidase
Background The protein encoded by this gene is a cysteine-aspartic acid protease that plays a central role in the execution-phase of cell apoptosis. The encoded protein cleaves and inactivates poly(ADP-ribose) polymerase while it cleaves and activates sterol regulatory element binding proteins as well as caspases 6, 7, and 9. This protein itself is processed by caspases 8, 9, and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. [provided by RefSeq, Aug 2017]
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. [UniProt]
Cellular Localization Cytoplasm. [UniProt]
Calculated MW 32 kDa
PTM 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. [UniProt]

Specific References

Mpox virus spreads from cell-to-cell and leads to neuronal injury in human cerebral organoids

IHC-Fr / Human

Isabel Schultz-Pernice et al.
BioRxiv,  (2023)

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KSR2-14-3-3ζ complex serves as a biomarker and potential therapeutic target in sorafenib-resistant hepatocellular carcinoma

WB / Human

Chao Gao et al.
Biomark Res,  (2022)

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