Caspase 9, p35, Human, Control Peptide (ICE-LAP6, Mch6, Apaf 3)

Article Name:	Caspase 9, p35, Human, Control Peptide (ICE-LAP6, Mch6, Apaf 3)
Biozol Catalog Number:	USB-C2088-23A
Supplier Catalog Number:	C2088-23A
Alternative Catalog Number:	USB-C2088-23A-100
Manufacturer:	US Biological
Category:	Molekularbiologie
Application:	ELISA

Apoptosis or programmed cell death is a fundamental cellular process that is essential for normal tissue development and abnormal growth such as cancer, neurodegeneration, autoimmune diseases, and angiogenesis, etc. Apoptosis is driven by specialized proteases known as caspases. After the initial discovery of the first mammalian caspase 1 or ICE (interleukin 1 beta converting enzyme), a growing family of caspases 1-14 have been cloned and characterized. Caspases are synthesized as inactive zymogen or proenzyme forms (30-55kD), which upon apoptotic stimulation are proteolytically processed (self or by other proteins) in a sequential manner into their active heterotetrameric forms. The processed form consists of large subunit (17-20kD) and a small (10-12kD) subunits, which may associate to form an active enzyme. Functionally active caspases initiate a proteolytic cascade, capable of cleaving and activating numerous cellular targets including PARP, G4-GDI, DFF, MEKK, etc. On a functional basis, two categories of caspases have been defined: the initiator caspases (caspases-8, -9, and -10) are activated in the earlier phases of apoptosis, whereas the executioner caspases (caspases-3, -6, and -7) are activated by initiator caspases and are responsible for dismantling cellular components. Caspases are widely distributed in various tissues and cells. Caspase-9 (rat/mouse 454 aa, human 416-aa, also known as apoptotic protease activating factor 3 (APAF-3)/ICE-like apoptotic protease 6 or ICE-LAP6 or MCH-6, is involved in the activation cascade of caspases responsible for apoptosis execution. Binding of Caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates caspase-3. Casp-9 proteolytically cleaves poly ADP-ribose polymerase (PARP). It is a heterodimer of a ~35kD (p35) and 10kD (p10) subunit. Proteolytic cleavages at Asp315 by granenzyme B and at Asp330 by CPP32 generate the two active subunits. Caspase-8 and -10 may also be involved in these processing events. Caspase-9 is ubiquitous with highest expression in the heart, and moderate expression in liver and skeletal muscle. Source: 25aa peptide of human Caspase-9 ~CT of p35 subunit Applications: Suitable for use in ELISA. Other applications not tested. Recommended Dilution: ELISA: Control peptide can be used to coat ELISA plates at 1ug/ml and detected with antibodies (1:10-50K for neat serum and 0.5-1ug/ml for affinity pure). Optimal dilution determined by the researcher. Storage and Stability: May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 6 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Purity:	Purified
Form:	Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide.