Anti-Human MD-1 Antibody

101-M566

Anti-Human MD-1 Antibody

MD1 is a secreted glycoprotein that is associated with RP105 and is required for efficient RP105 cell surface expression and function. RP105 is a type I transmembrane glycoprotein with extracellular leucine rich repeats (LRR) typically found in Toll-like receptor (TLR) family members. However, RP105 has a short cytoplasmic tail and lacks the Toll-IL1 R (TIR) domain that defines the IL1 R/TLR superfamily. RP105 plays an important role in B-cell activation by bacterial lipopolysaccharide (LPS). It is expressed primarily on mature B cells, dendritic cells and macrophages. Human MD1 cDNA encodes a 162 amino acid (aa) precursor protein with a putative 19 aa signal peptide and two potential N-linked glycosylation sites. It shares 38% and 66% amino acid sequence identity with chicken and mouse MD1 respectively. MD1 is mainly expressed in spleen, and also detectable in liver, brain, thymus, and kidney. The cell surface RP105/MD 1 complex, in conjunction with TLR4, mediates the innate immune response to LPS in B cells. Activation of the RP105 complex has been shown to protect against apoptosis, induce B-cell proliferation and upregulate B7.2, a costimulatory molecule. Since MD1 is also expressed in liver and brain where RP105 is absent, MD1 may also be associated with other LRR-containing molecules, or have additional functions outside the immune system.

748.5 €

101-M567

Anti-Human MD-2 Antibody

MD-2, also known as lymphocyte antigen 96 and ESOP-1, is a secreted glycoprotein that associates with the extracellular domain of TLR-4. MD-2 is required for LPS binding and subsequent TLR-4 signaling.

748.5 €

hAP-0468

Mouse Monoclonal anti-human MD-1

525 €

102-PA138S

Anti-Human Mdg-1 Antibody

Angiogenesis research has focused on receptors and ligands mediating endothelial cell proliferation and migration. Little is known about the molecular mechanisms that are involved in converting endothelial cells from a proliferative to a differentiated state. Microvascular differentiation gene 1 (Mdg1) has been isolated from differentiating microvascular endothelial cells that had been cultured in collagen type I gels (3D culture). In adult human tissue Mdg1 is expressed in endothelial and epithelial cells. Sequence analysis of the full-length cDNA revealed that the N-terminal region of the putative Mdg1-protein exhibits a high sequence similarity to the J-domain of Hsp40 chaperones. It was shown that this region functions as a bona fide J-domain as it can replace the J-domain of Escherichia coli DnaJ-protein. Mdg1 is also upregulated in primary endothelial and mesangial cells when subjected to various stress stimuli. GFP–Mdg1 fusion constructs showed the Mdg1-protein to be localized within the cytoplasm under control conditions. Stress induces the translocation of Mdg1 into the nucleus, where it accumulates in nucleoli. Costaining with Hdj1, Hdj2, Hsp70, and Hsc70 revealed that Mdg1 colocalizes with Hsp70 and Hdj1 in control and stressed HeLa cells. These data suggest that Mdg1 is involved in the control of cell cycle arrest taking place during terminal cell differentiation and under stress conditions.

339 €

102-PA23

Anti-Human NRP-1 Antibody

Neuropilin-1 (NRP-1, CD304) is a 130-140 kDa type I transmembrane glycoprotein that regulates axon guidance and angiogenesis. The human NRP-1 contains a 623 aa extracellular domain (ECD) that shows 92-95% aa identity with mouse, rat, bovine and canine NRP-1. The ECD contains two N-terminal CUB domains (termed a1a2), two domains with homology to coagulation factors V and VIII (b1b2) and a MAM (meprin) domain. C-terminally divergent splice variants with 704, 644, 609, and 551 aa lack the MAM and TM domains and are demonstrated or presumed to be soluble antagonists. Heparin, the heparin-binding forms of VEGF (VEGF165, VEGF-B; VEGF-E), PlGF-2, and the C-terminus of Sema3 bind the b1b2 region. NRP-1 and NRP-2 share 48% aa identity within the ECD and can form homo and hetero-oligomers via interaction of their MAM domains. Neuropilins show partially overlapping expression in neuronal and endothelial cells during development. Both neuropilins act as coreceptors with Plexins, mainly Plexin A3 and A4, to bind class III Semaphorins that mediate axon repulsion. However, only NRP-1 binds Sema3A, and only NRP-2 binds Sema 3F. Both are co-receptors with VEGFR-2 (KDR7Flk1) for VEGF165 binding. Sema 3A signaling can be blocked by VEGF165, which has higher affinity for NRP-1. NRP-1 is preferentially expressed in arteries during development or those undergoing remodeling. NRP-1 is also expressed on dendritic cells and mediates DC-induced T-cell proliferation

457.12 €

102-PA23AG

Anti-Human NRP-1 Antibody

Neuropilin-1 (NRP-1, CD304) is a 130-140 kDa type I transmembrane glycoprotein that regulates axon guidance and angiogenesis. The human NRP-1 contains a 623 aa extracellular domain (ECD) that shows 92-95% aa identity with mouse, rat, bovine and canine NRP-1. The ECD contains two N-terminal CUB domains (termed a1a2), two domains with homology to coagulation factors V and VIII (b1b2) and a MAM (meprin) domain. C-terminally divergent splice variants with 704, 644, 609, and 551 aa lack the MAM and TM domains and are demonstrated or presumed to be soluble antagonists. Heparin, the heparin-binding forms of VEGF (VEGF165, VEGF-B; VEGF-E), PlGF-2, and the C-terminus of Sema3 bind the b1b2 region. NRP-1 and NRP-2 share 48% aa identity within the ECD and can form homo and hetero-oligomers via interaction of their MAM domains. Neuropilins show partially overlapping expression in neuronal and endothelial cells during development. Both neuropilins act as coreceptors with Plexins, mainly Plexin A3 and A4, to bind class III Semaphorins that mediate axon repulsion. However, only NRP-1 binds Sema3A, and only NRP-2 binds Sema 3F. Both are co-receptors with VEGFR-2 (KDR7Flk1) for VEGF165 binding. Sema 3A signaling can be blocked by VEGF165, which has higher affinity for NRP-1. NRP-1 is preferentially expressed in arteries during development or those undergoing remodeling. NRP-1 is also expressed on dendritic cells and mediates DC-induced T-cell proliferation

386.25 €