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Product Details
BMS1040
Applications
Tested Dilution
Publications
Product Specifications
Species Reactivity
Human
Host/Isotype
Mouse
/ IgG2a
Class
Monoclonal
Type
Antibody
Clone
MAR-1
Immunogen
Rec. Human Caspase-3
Conjugate
Form
Liquid
Concentration
1 mg/mL
Purification
Affinity chromatography
Storage buffer
PBS, pH 7.2-7.4
Contains
no preservative
Storage conditions
-20°C
Shipping conditions
Wet ice
RRID
AB_10598524
Product Specific Information
Description: Caspases are present in all cells, recruitment of these proteases to oligomerized receptors leads to activation accompanied by autoproteolytic cleavage. Active caspases can proteolyze additional caspases generating a caspase cascade that cleaves proteins critical for cell survival. The final outcome of this signaling pathway is a form of controlled cell death termed apoptosis. The subgroup of caspases involved in apoptosis is called initiators or effectors. Caspase-3 cleaves substrate at the carboxyl terminus of aspartate residues. Active caspase-3 has two active sites and consists of two identical large (~ 20 kDa) and two identical small (~ 10 kDa) subunits that are derived from two precursor caspase-3 polypeptides. Caspase-3 is proteolytically activated by other caspases.
Both subunits contribute to substrate binding and catalysis. The active site cysteine that covalently binds the substrate is located near the C-terminus of the large subunit. Active caspase-3 has two-fold symmetry, two active site pockets each residing on an opposite side. Caspase-3, together with caspases 8 and 9, is situated at pivotal junctions in apoptotic pathways. Caspase-3 appears to amplify caspase 8 and 9 initiation signals into complete commitment to apoptotic disassembly.
Applications Tested: ELISA, Western Blotting.
Target Information
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: Apopain; Apopain precursor; CASP-3; caspase 3, apoptosis-related cysteine peptidase; caspase 3, apoptosis-related cysteine protease; Caspase-3; Caspase3; CPP-32; Cysteine protease CPP32; ICE3; PARP cleavage protease; procaspase3; Protein Yama; SCA-1; SREBP cleavage activity 1
Gene Aliases: CASP3; CPP32; CPP32B; SCA-1
UniProt ID: (Human) P42574
Entrez Gene ID: (Human) 836
protease binding
aspartic-type endopeptidase activity
cysteine-type endopeptidase activity
cyclin-dependent protein serine/threonine kinase inhibitor activity
death receptor binding
protein binding
peptidase activity
cysteine-type endopeptidase activator activity involved in apoptotic process
phospholipase A2 activator activity
protein complex binding
cysteine-type endopeptidase activity involved in apoptotic process
cysteine-type endopeptidase activity involved in execution phase of apoptosis
protease
response to hypoxia
B cell homeostasis
apoptotic DNA fragmentation
proteolysis
apoptotic process
activation of cysteine-type endopeptidase activity involved in apoptotic process
cellular component disassembly involved in execution phase of apoptosis
cellular response to DNA damage stimulus
heart development
sensory perception of sound
learning or memory
activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c
response to UV
response to glucose
response to X-ray
regulation of macroautophagy
protein processing
hippocampus development
neuron differentiation
keratinocyte differentiation
erythrocyte differentiation
platelet formation
negative regulation of B cell proliferation
response to cobalt ion
response to estradiol
response to lipopolysaccharide
glial cell apoptotic process
response to tumor necrosis factor
response to nicotine
hippo signaling
wound healing
response to drug
response to hydrogen peroxide
T cell homeostasis
negative regulation of apoptotic process
response to amino acid
positive regulation of neuron apoptotic process
cell fate commitment
negative regulation of cyclin-dependent protein serine/threonine kinase activity
negative regulation of activated T cell proliferation
response to antibiotic
neurotrophin TRK receptor signaling pathway
response to glucocorticoid
neuron apoptotic process
cellular response to organic cyclic compound
apoptotic signaling pathway
extrinsic apoptotic signaling pathway in absence of ligand
execution phase of apoptosis
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