Rabbit Caspase 3, Active/Cleaved Polyclonal Antibody | anti-CASP3 antibody

Caspase 3, Active/Cleaved (Caspase-3, CASP 3, CASP3, CASP-3, CPP-32, Apopain, Yama, SCA-1, ASP3, Apoptosis-related Cysteine Peptidase Apopain, Apopain, Cysteine Protease CPP32, SREBP Cleavage Activity 1)

Cat. Num. AAA6005687

• Gene Names: CASP3; CPP32; SCA-1; CPP32B
• Reactivity: canine, gerbil, mouse and rat
• Applications: Western Blot, Immunoprecipitation, Immunohistochemistry
• Purity: Serum; Serum
• Synonyms: Caspase 3; Active/Cleaved; Polyclonal Antibody; Active/Cleaved (Caspase-3; CASP 3; CASP3; CASP-3; CPP-32; Apopain; Yama; SCA-1; ASP3; Apoptosis-related Cysteine Peptidase Apopain; Cysteine Protease CPP32; SREBP Cleavage Activity 1); Anti -Caspase 3; SREBP Cleavage Activity 1; Yama Protein); anti-CASP3 antibody

• Host: Rabbit
• Reactivity: canine, gerbil, mouse and rat
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: Recognizes the large (~14-21kD) and small (~10kD) subunits of human active/cleaved caspase-3. Nuclear immunostaining of Caspase-3 is considered to be an indication of active/cleaved caspase-3. May also recognize the pro-form of caspase-3 (~32kD).
• Purity/Purification: Serum; Serum
• Form/Format: Supplied as a liquid, 0.05% sodium azide.

• Applicable Applications for anti-CASP3 antibody: Western Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC)
• Application Notes: Suitable for use in Western Blot, Immunohistochemistry and Immunoprecipitation.; Dilution: Western Blot: 1:1000-1:2000; Immunohistochemistry (FFPE): 1:1000-1:5000; Immunohistochemistry: Frozen sections; Immunoprecipitation: 1:50-1:200
• Immunogen: Recombinant corresponding to catalytically active human caspase-3 protein.
• Positive Control: Cells or tissues undergoing apoptosis, lymphatic tissues, ischemic brain
• Preparation and Storage: May be stored at 4 degree C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degree C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Immunohistochemistry (IHC)

(Immunohistochemistry Analysis: Formalin-fixed, paraffin-embedded section of dog ischemic brain using MBS6005687 (1:2000). Staining is seen in the nuclei of dying neurons (black arrow) but not in the morphologically normal nuclei (open arrows). Caspase-3 expression in the nucleus is considered to be a marker of active/caspase-3 expression and apoptosis. Hematoxylin-eosin counterstain.)

Immunohistochemistry (IHC)

(Immunohistochemistry Analysis: Formalin-fixed, paraffin-embedded section of irradiated mouse spleen using MBS6005687 (1:2000). Staining is seen in the nuclei of a subset of the cell population. Caspase-3 expression in the nucleus is considered to be a marker of active/caspase-3 expression and apoptosis. Hematoxylin-eosin counterstain.)

Related Product Information for anti-CASP3 antibody

Apoptosis, or programmed cell death, is a common property of all multicellular organisms. The current dogma of apoptosis suggests that the components of the core cell-death machinery are integral to cells and widely conserved across species. Caspases, a family of cysteinyl aspartate-specific proteases, are integral components of the cell death machinery (reviewed in Siegal, 2006; and Lavrik et al, 2005). They play a central role in the initiation and execution of apoptotic cell death and in inflammation. Caspases are typically divided into 3 major groups, depending on the structure of their prodomain and their function. Group 1: inflammatory caspases (caspases 1, 4, 5, 11, 12, 14). Group II: initiator of apoptosis caspases (caspases 2, 8, 9). Group II: effector caspases (caspases 3, 6, 7). Caspases are synthesized as zymogens (inactive pro enzyme precursors which require a biochemical change to become active enzymes) with an N-terminal prodomain of variable length followed by a large subunit (p20) and a small subunit (p10). Caspases are activated through proteolytic cleavage at specific asparagine residues that are located within the prodomain, the p10, and p20 subunits. Activation results in the generation of mature active caspases that consist of the heterotetramer p202-p102.

Product Categories/Family for anti-CASP3 antibody

Antibodies; Abs to Apoptosis; Caspase

NCBI and Uniprot Product Information

• NCBI GI #: 14790119
• NCBI GeneID: 836
• NCBI Accession #: NP_004337.2
• NCBI GenBank Nucleotide #: NM_004346.3
• UniProt Accession #: P42574; Q96AN1; Q96KP2; A8K5M2; D3DP53
• NCBI Official Full Name: caspase-3 preproprotein
• NCBI Official Synonym Full Names: caspase 3, apoptosis-related cysteine peptidase
• NCBI Official Symbol: CASP3
• NCBI Official Synonym Symbols: CPP32; SCA-1; CPP32B
• NCBI Protein Information: caspase-3; CASP-3; CPP-32; apopain; procaspase3; protein Yama; PARP cleavage protease; cysteine protease CPP32; SREBP cleavage activity 1; caspase 3, apoptosis-related cysteine protease
• UniProt Protein Name: Caspase-3
• Protein Family: Caspase
• UniProt Gene Name: CASP3
• UniProt Synonym Gene Names: CPP32; CASP-3; CPP-32; SCA-1
• UniProt Entry Name: CASP3_HUMAN

NCBI Description

This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the 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. Alternative splicing of this gene results in two transcript variants that encode the same protein. [provided by RefSeq, Jul 2008]

Uniprot Description

CASP3: 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. Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. Interacts with BIRC6/bruce. 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. Inhibited by isatin sulfonamides. Belongs to the peptidase C14A family.

Protein type: Apoptosis; Motility/polarity/chemotaxis; Protease; EC 3.4.22.56

Chromosomal Location of Human Ortholog: 4q34

Cellular Component: nucleoplasm; plasma membrane; cytosol; nucleus

Molecular Function: cyclin-dependent protein kinase inhibitor activity; peptidase activity; protein binding; cysteine-type endopeptidase activity; aspartic-type endopeptidase activity

Biological Process: extracellular matrix organization and biogenesis; nerve growth factor receptor signaling pathway; positive regulation of apoptosis; apoptosis; heart development; negative regulation of activated T cell proliferation; negative regulation of B cell proliferation; regulation of caspase activity; proteolysis; neuron differentiation; extracellular matrix disassembly; sensory perception of sound; B cell homeostasis; positive regulation of neuron apoptosis; response to wounding; erythrocyte differentiation; T cell homeostasis; DNA fragmentation during apoptosis; cell structure disassembly during apoptosis; response to UV; release of cytochrome c from mitochondria; cell fate commitment; negative regulation of cyclin-dependent protein kinase activity; keratinocyte differentiation; neuron apoptosis; induction of apoptosis via death domain receptors; platelet formation; caspase activation via cytochrome c; induction of apoptosis by oxidative stress; response to DNA damage stimulus; negative regulation of apoptosis