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Livin peptide
Livin peptide
Tax included
Apoptosis, or programmed cell death, is related to many diseases, such as cancer. Apoptosis is triggered by a variety of stimuli including members in the TNF family and prevented by the inhibitor of apoptosis (IAP) proteins. IAP proteins form a conserved gene family that binds to and inhibits cell death proteases. A novel member in the IAP protein family was recently identified and designated Livin and KIAP for kidney IAP. Livin / XIAP contains a single baculoviral IAP repeat (BIR) domain and a RING finger domain and has two isoforms termed Livin alpha and Livin beta. Transfection of Livin in cells resulted in protection from apoptosis induced by FADD, BAX, RIP, RIP 3 and DR6. Livin has direct interaction with several caspases including caspase 3, 7, and 9. Livin inhibits the activation of caspase 9 induced by Apaf 1, cytochrome c, and dATP. The two isoforms of Livin appear to have different functions and tissue distributions.
Product Details
Brand:
Genetex
Reference:
GTX26234
Data sheet
Size
50μg
Conjugation
Unconjugated
Application
Neutralizing/Inhibition
URL - Product
https://www.genetex.com/Product/Detail/Livin-peptide/GTX26234
Apoptosis, or programmed cell death, is related to many diseases, such as cancer. Apoptosis is triggered by a variety of stimuli including members in the TNF family and prevented by the inhibitor of apoptosis (IAP) proteins. IAP proteins form a conserved gene family that binds to and inhibits cell death proteases. A novel member in the IAP protein family was recently identified and designated Livin and KIAP for kidney IAP. Livin / XIAP contains a single baculoviral IAP repeat (BIR) domain and a RING finger domain and has two isoforms termed Livin alpha and Livin beta. Transfection of Livin in cells resulted in protection from apoptosis induced by FADD, BAX, RIP, RIP 3 and DR6. Livin has direct interaction with several caspases including caspase 3, 7, and 9. Livin inhibits the activation of caspase 9 induced by Apaf 1, cytochrome c, and dATP. The two isoforms of Livin appear to have different functions and tissue distributions.
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