Abcam, ab198447, Recombinant human Cleaved Caspase-3 protein

Size: 50µg
Recombinant human Cleaved Caspase-3 protein is a Human Full Length protein, in the 1 to 277 aa range, expressed in Escherichia coli, with >99%, suitable for SDS-PAGE, FuncS.
Key facts
Purity:>99% SDS-PAGE,
Expression system:Escherichia coli,
Tags:His tag C-Terminus,
Applications:FuncS, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:Yes,
Biological activity:Specific Activity: ≥ 6,784 pmol/min/μg,
Accession:P42574,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 20% Glycerol (glycerin, glycerine), 0.64% Sodium chloride, 0.63% Tris HCl, 0.05% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.04% Sorbitan monolaurate, ethoxylated, 0.02% Potassium chloride

Product details:
Useful for the study of enzyme kinetics, screening inhibitors,and selectivity profiling.

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The Cleaved Caspase-3 also known as active caspase 3 plays an important role in the execution phase of cell apoptosis. The caspase 3 molecule has a molecular weight of approximately 32 kDa. It undergoes cleavage into subunits that are important for its activation marking its conversion into the cleaved form. Cleaved caspase is widely expressed in various tissues with a notable presence in the cytoplasm of cells undergoing apoptotic processes. Cleavage of caspase 3 results in the formation of a functional enzyme that participates in the degradation of cellular components during apoptosis.
Biological function summary
Caspase 3 acts as an executioner enzyme in the process of programmed cell death. Its cleavage from the inactive zymogen form into the active form triggers apoptotic pathways ensuring the removal of damaged or unnecessary cells. Cleaved caspase operates within a proteolytic cascade often in conjunction with other caspases such as caspase 9. Once activated caspase 3 targets and cleaves specific cellular substrates contributing to the characteristic morphological changes and DNA fragmentation associated with apoptosis.
Pathways
Cleaved caspase 3 is significant within the intrinsic and extrinsic apoptotic pathways. It acts downstream of initiator caspases such as caspase 9 in the intrinsic pathway where its activation involves mitochondrial signals. In the extrinsic pathway it closely associates with caspase 8 mediating cell death signals from extracellular triggers. These pathways ensure that cleaved caspase 3 fulfills its role as a critical mediator of apoptosis linking upstream death signals to cellular dismantling during the apoptosis process.
Cleaved caspase 3 connects to conditions such as cancer and neurodegenerative diseases. In cancer dysregulation of caspase 3 activity may lead to evasion of apoptosis facilitating tumor progression. Therapeutic approaches aim to restore its apoptotic functions in cancer cells. In neurodegenerative diseases like Alzheimer's disease abnormal activation of cleaved caspase 3 contributes to neuronal loss. It interacts with proteins like amyloid precursor protein promoting the pathological changes associated with this disorder. Understanding these interactions provides insights into potential therapeutic avenues.