DC-SIGN peptide Reference: GTX26091 Dendritic cells (DCs) that control immune responses were recently found to capture and transport HIV from the mucosal area to remote lymph nodes, where DCs hand over HIV to CD4+ T lymphocytes. DCs also amplify the amount of virus and extend the duration of viral infectivity. Multiple strains of HIV-1, HIV-2 and SIV bind to DCs via DCSIGN (also termed CD29). ICAM-3 is the natural ligand for DC-SIGN. A DC-SIGN homologue (termed DC-SIGNR, L-SIGN, and DCSIGN2) was identified recently. DC-SIGN forms a novel gene family with DC-SIGNR and many alternatively spliced isoforms of DC-SIGN and DC-SIGNR. The expression of DC-SIGN was found in mucosal tissues including placenta, small intestine, and rectum.
DC-SIGN peptide Reference: GTX26092 Dendritic cells (DCs) that control immune responses were recently found to capture and transport HIV from the mucosal area to remote lymph nodes, where DCs hand over HIV to CD4+ T lymphocytes. DCs also amplify the amount of virus and extend the duration of viral infectivity. Multiple strains of HIV-1, HIV-2 and SIV bind to DCs via DCSIGN (also termed CD29). ICAM-3 is the natural ligand for DC-SIGN. A DC-SIGN homologue (termed DC-SIGNR, L-SIGN, and DCSIGN2) was identified recently. DC-SIGN forms a novel gene family with DC-SIGNR and many alternatively spliced isoforms of DC-SIGN and DC-SIGNR. The expression of DC-SIGN was found in mucosal tissues including placenta, small intestine, and rectum.
DcR1 peptide Reference: GTX26096 Apoptosis is induced by certain cytokines including TNF and Fas ligand in the TNF family through their death domain containing receptors. TRAIL/Apo2L is a new member of the TNF family and induces apoptosis of a variety of tumor cell lines. DR4 and DR5 are the recently identified functional receptors for TRAIL. Two decoy receptors for TRAIL have been identified and designated DcR1/TRID/TRAIL-R3/LIT and DcR2/TRAIL-R4/TRUNDD. DcR1 has extracellular TRAIL-binding domain but lacks intracellular signaling domain. It is a glycophospholipid-anchored cell surface protein. DcR1 transcripts are expressed in many normal human tissues but not in most cancer cell lines. Overexpression of DcR1 did not induce apoptosis, but attenuated TRAIL-induced apoptosis.
DEDAF peptide Reference: GTX26097 Cell death signal are transduced by Death Domain (DD), Death Effector Domain (DED), and Caspase Recruitment Domain (CARD) containing molecules. A novel protein that interacts with DED of caspase-8 and -1, and FADD was recently identified and designated DEDAF (for DED associated factor). DEDAF is identical to the transcriptional repressor RYBP. DEDAF interacts with FADD and augments the formation of CD95/FADD/caspase-8 complexes at the cytoplasm. DEDAF also interacts with DED-containing DNA binding protein (DEDD) in the nucleus, indicating it is involved in the regulation of both cytoplasmic and nuclear events of apoptosis.
F1A alpha peptide Reference: GTX26098 F1A alpha, also termed FEM1 beta, is a novel protein that associates with the intracellular domains of Fas and TNFR1. Over expression of F1A alpha induces apoptosis. F1A alpha also associates with CED-4 and its mammalian homologue Apaf-1, and can be cleaved by CED-3 and caspases.
sRANKL, rat, recombinant Reference: E-63200 Recombinant Rat soluble Receptor Activator of NF-Kappa-B Ligand
GDNF Receptor alpha 1 peptide Reference: GTX26099 Glial cell line-derived neurotrophic factor (GDNF) is a potent survival factor for central and peripheral neurons and is essential for the development of kidneys and the enteric nervous system. Physiological responses to GDNF require the presence of a novel glycosylphosphadidylinositol linked protein GDNFRa, which is a cell surface receptor for GDNF. The cDNAs encoding GDNFRa from human, rat, chicken and mouse have been cloned recently. GDNFRa was also termed Ret ligand 1 (RETL1) or TGF-b-related neurotrophic factor receptor 1 (TrnR1) and nominated as GFRa-1. GFRa-1 binds GDNF specifically and mediates activation of the Ret protein tyrosine kinase (PTK). Thus, GDNF, GFRa and the Ret PTK form a complex to transduce GDNF signal and to mediate GDNFfunction.