coagulation factor II (thrombin) B chain fragment [Homo sapiens] Reference: A1057-5 Trypsin-like serine protease
CXCR4 peptide Reference: GTX28126 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.
coagulation factor II (thrombin) B chain fragment [Homo sapiens] Reference: A1057-10 Trypsin-like serine protease
Eotaxin peptide Reference: GTX28127 Eotaxin is a 74-amino acid, eosinophil-chemotactic CC chemokine originally found in bronchoalveolar lavage fluid from allergic inflammatory subjects. It is involved in regulating the recruitment and activation of inflammatory leukocytes, particularly eosinophils. Eotaxin binds and activates the CCR3 chemokine receptor, and may play a fundamental role in the development of allergic responses.
coagulation factor II (thrombin) B chain fragment [Homo sapiens] Reference: A1057-25 Trypsin-like serine protease
FLIP peptide Reference: GTX28129 The human homolog of viral FLIP has four splice variants known as FLIP alpha, Beta, gamma and kappa. These are FLICE inhibitory proteins also known as Casper, I-FLICE, FLAME-1, CASH, CLARP and Usurpin. They contain two death effector domains and one caspase domain. FLIP interacts
PATJ blocking peptide Reference: GTX28225-PEP This gene encodes a protein with multiple PDZ domains. PDZ domains mediate protein-protein interactions, and proteins with multiple PDZ domains often organize multimeric complexes at the plasma membrane. This protein localizes to tight junctions and to the apical membrane of epithelial cells. A similar protein in Drosophila is a scaffolding protein which tethers several members of a multimeric signaling complex in photoreceptors. [provided by RefSeq, Jul 28]
Acinus peptide Reference: GTX28367 Chromatin condensation and nuclear fragmentation (CCNF)is the hallmark of apoptosis. CCNF is triggered by the activation of members of caspase family, caspase activated DNase (CAD/DFF4), and several novel proteins including AIF and CIDE. A new inducer of chromatin condensation was recently identified and designated Acinus (for apoptotic chromatin condensation inducer in the nucleus). Acinus is cleaved by caspase-3 and an additional unknown protease generating a small active peptide p17, which causes chromatin condensation in vitro when it is added to purified nuclei. Acinus also induces apoptotic chromatin condensation in cells. Acinus is ubiquitously expressed. Three different spliced forms of Acinus have been identified in human and mouse and designated AcinusL, AcinusS and AcinusS.
Acinus peptide Reference: GTX28368 Chromatin condensation and nuclear fragmentation (CCNF)is the hallmark of apoptosis. CCNF is triggered by the activation of members of caspase family, caspase activated DNase (CAD/DFF4), and several novel proteins including AIF and CIDE. A new inducer of chromatin condensation was recently identified and designated Acinus (for apoptotic chromatin condensation inducer in the nucleus). Acinus is cleaved by caspase-3 and an additional unknown protease generating a small active peptide p17, which causes chromatin condensation in vitro when it is added to purified nuclei. Acinus also induces apoptotic chromatin condensation in cells. Acinus is ubiquitously expressed. Three different spliced forms of Acinus have been identified in human and mouse and designated AcinusL, AcinusS and AcinusS.