85-1402-05　Livin, Human (ML-IAP) Control Peptide 100ug　L3180-50

特徴

• 15-aa peptide from human Livin .
• 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 (Cysteine Aspartase). The inhibitor-of-apoptosis protein (IAPs) by virtue of inhibiting caspase activity has widespread anti-apoptotic potential family. IAPs are characterized by one or more repeats of a highly conserved ~70 amino acid domain termed the baculoviral IAP repeat (BIR). There are at least five human IAP family members, c-IAP1, c-IAP2, XIAP, NAIP, and survivin. All of the human IAP family members, with the exception of NAIP, have been shown to interact with specific cysteine proteases, or caspases. The caspases are synthesized as inactive zymogen forms which upon apoptotic stimulation are proteolytically processed in a sequential manner into their active heterotetrameric forms. The BIR domain is critical motif for anti-apoptotic activity and interaction with caspases. Many of the IAPs also contain a RING domain near their COOH-termini that is not required for the anti-apoptotic activity.
• A novel member of the IAPs, termed livin (also known as IAP kidney or KIAP; IAP melanoma or MLIAP), encodes a protein with a single BIR domain and a COOH-terminal RING domain. Expression of livin inhibited apoptosis by a number of stimuli. Livin can bind to caspases and it could inhibit the proteolytic processing of caspase-9 in vitro. Livin gene (chromosome 20q13.3) encodes a 280 amino acid protein. It has 25-35% identity with other IAP family members (c-IAP1, c-IAP2, XIAP, NAIP, and surviving). At a structural level it was similar to survivin with respect to having just a single BIR domain. However, livin did not have a coiled-coil domain like survivin, but rather contained a COOH-terminal RING domain found in c-IAP1, c-IAP2, and XIAP. Livin gene has two splicing variants that contain open reading frames of 298 and 280 amino acids and both contained a single copy of baculovirus IAP repeat (BIR) and RING domain. Both of the isoforms inhibit TNFa induced apoptosis in Jurkat cells. Livin expression is low in adult tissues. It is relatively expressed at a higher level in developmental tissues and in many cancer cells. Livin was not detectable in most normal adult tissues with the exception of the placenta, but was present in fetal brain and in several cancer cell lines (melanoma-derived cell lines, G361 and SK-Mel29.