Caspase 8 Mouse, Control Peptide (FLICE, CASP-8, FLICE, ICE-like apoptotic protease 5, MACH, MCH5)

Referentie C2087-42E-100ug

Formaat : 100ug

Merk : US Biological



C2087-42E Caspase 8 Mouse, Control Peptide (FLICE, CASP-8, FLICE, ICE-like apoptotic protease 5, MACH, MCH5)

Grade
Purified
Applications
E
Shipping Temp
Blue Ice
Storage Temp
-20°C

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-8, also known as (MACH, FADD-like ICE, FLICE, Mch-5, CAP4, MACH-alpha 1) human proenzyme is 479 aa (mouse 480 aa, rat 482 aa). It is the most upstream protease of the activation of caspases responsible for CD95 and TNFR-1 induced cell death. It cleaves and activates caspases-3, -4, -6, -7, -9, and –10. It is a heterodimer of a 19kD (p18) and 10kD (p10) subunits. Caspase-8 is alternatively spliced into at least 8 isoforms (1-4 alpha, 1-4 beta). Alpha 1 and beta-1 are expressed in a many tissues. Highest expression is observed in peripheral blood, leukocytes, spleen, thymus and liver. Lower expression is seen in brain and testis.

Source:
15aa peptide within the p18 domain of human Caspase-8 p18 domain

Applications:
Suitable for use in Western Blot and ELISA. Other applications not tested.

Recommended Dilution:
ELISA: 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).

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, store at -20°C. Aliquots are stable for at least 6 months at -20°C. 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.

Applications
Source: Mouse synthetic peptide|Purity: Purified|Concentration: ~1mg/ml|Form: Supplied as a liquid in PBS, pH 7.2, 0.1% sodium azide.|Specificity: Human control peptide is 69% conserved in mouse caspase-8. No significant sequence homology is detected with other caspases.||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Form
Supplied as a liquid in PBS, pH 7.2, 0.09% sodium azide.
Purity
Purified
Specificity
Human control peptide is 69% conserved in mouse caspase-8. No significant sequence homology is detected with other caspases.
References
1.) Boldin MP et al (1996) Cell, 85, 803;|2.) Muzio M et al (1996) Cell 85, 817;|3.) Grenet J et al (1999) Gene 226, 225-232;|4.) Van de Craen et al (1999) Gene accession # AJ007749