Category: Proteins & Peptides

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AIF peptide

Reference: GTX27871

This gene encodes a flavoprotein essential for nuclear disassembly in apoptotic cells, and it is found in the mitochondrial intermembrane space in healthy cells. Induction of apoptosis results in the translocation of this protein to the nucleus where it affects chromosome condensation and fragmentation. In addition, this gene product induces mitochondria to release the apoptogenic proteins cytochrome c and caspase-9. Mutations in this gene cause combined oxidative phosphorylation deficiency 6 (COXPD6), a severe mitochondrial encephalomyopathy, as well as Cowchock syndrome, also known as X-linked recessive Charcot-Marie-Tooth disease-4 (CMTX-4), a disorder resulting in neuropathy, and axonal and motor-sensory defects with deafness and cognitive disability. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 1. [provided by RefSeq, Aug 215]

APAF1 peptide

Reference: GTX27872

Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. The mammalian homolog of the key cell death gene CED 4 in C. elegans was identified recently from human and mouse and designated APAF1 for Apoptosis protease-activating factor 1. APAF1 binds to Cytochrome c (APAF2) and Caspase 9 (APAF3), which leads to Caspase 9 activation. Activated Caspase 9 in turn cleaves and activates Caspase 3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. APAF1 can also associate with Caspase 4 and Caspase 8. APAF1 transcript is ubiquitously expressed in human tissues.

APAF1 peptide

Reference: GTX27873

Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. The mammalian homolog of the key cell death gene CED 4 in C. elegans was identified recently from human and mouse and designated APAF1 for Apoptosis protease-activating factor 1. APAF1 binds to Cytochrome c (APAF2) and Caspase 9 (APAF3), which leads to Caspase 9 activation. Activated Caspase 9 in turn cleaves and activates Caspase 3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. APAF1 can also associate with Caspase 4 and Caspase 8. APAF1 transcript is ubiquitously expressed in human tissues.

CCR5 peptide

Reference: GTX27876

Receptors for the CC chemokine family include CCR1, CCR2A, CCR3, CCR4, CCR5 and the Duffy blood group antigen. The CC receptors are important in the function of T cell chemotaxis and migration of phagocytic cells to sites of inflammation. The HIV receptor is composed of two molecules, the CD4 binding receptor and a co receptor. The chemokine receptor CCR5 is one of the co receptors used by primary isolates of HIV1. Extracellular domains of CCR5 are important for HIV entry into the target cells.

CXCR4 peptide

Reference: GTX27877

CXCR4 (fusin, LESTR or HUMSTR) is a principal coreceptor for T-cell tropic strains of HIV-1 fusion and entry of human white blood cells. CXCR4 is also required for the infection by dual-tropic strains of HIV-1 and mediates CD4 independent infection by HIV-2. The a-chemokine SDF-1 is the ligand for CXCR4 and prevents infection by T-tropic HIV-1. CXCR4 associates with the surface CD4-gp12 complex before HIV enters target cells. CXCR4 messenger RNA levels correlated with HIV-1 permissiveness in diverse human cell types. Antibodies to CXCR4 block HIV-1 and HIV-2 fusion and infection of human target cells. The amino-terminal domain and the second extracellular loop of CXCR4 serve as HIV biding sites.CXCR4 is highly expressed in brain and heart, and in white blood cells, vascular endothelial cells, and umbilical cord endothelial cells.

MyD88 peptide

Reference: GTX27878

Myeloid differentiation Marker 88 (MyD88) is an adaptor molecule for the Toll/IL-1R and is involved in the inflammatory response induced by IL-1, IL-18 and LPS. MyD88 recruits IRAK to IL-1 receptor complex in response to IL-1. This pathway further leads to activation of NF-kB. MyD88 has a wide tissue distribution.

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