Anti-Human Mdg-1 Antibody ReliaTech

Anti-Human Mdg-1 Antibody

457.12 EUR

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Katalognummer: 209 - 102-PA138

Produktkategori: Företag och industri > Vetenskap och laboratorium

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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.

457.12 €

102-PA138S

Anti-Human Mdg-1 Antibody

339 €

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 €

102-PA33S

Anti-Human Dkk-1 Antibody

DKK-1 is a member of the DKK protein family which also includes DKK-2, DKK-3 and DKK-4. DKK-1 was originally identified as a Xenopus head forming molecule that behaves as an antagonist for Wnt signaling. Subsequent studies have shown that DKK-1 and DKK-4 play an important regulatory role in the Wnt /β-catenin signaling pathway by forming inhibitory complexes with LDL receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/βcatenin signaling system. LPR5 and LPR6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/βcatenin signaling cascade. It has been suggested that by inhibiting Wnt/β-catenin signaling, which is essential for posterior patterning in vertebrates, DKK-1 permits anterior development. This notion is supported by the finding that mice deficient of DKK-1 expression lack head formation and die during embryogenesis. Recombinant human DKK-1 fused to a C terminal His-tag derived from E. coli is a 26 kDa protein containing 235 amino-acid residues.

339 €

102-PA48

Anti-Human ESL-1 Antibody

E-Selectin ligand-1/ESL-1 (GLG1, Golgi complex-Localized Glycoprotein 1; CFR1, MG160 and Cysteine-rich FGF receptor) is a 150-160 kDa glycoprotein. The amino acid sequence of MG160, a membrane sialoglycoprotein of the medial cisternae of the rat Golgi apparatus, is more than 90% identical with CFR, a fibroblast growth factor (FGF) binding protein of chicken membranes, and with ESL-1, a ligand for E-selectin of plasma membranes of myeloid cells; furthermore, MG160, isolated by immunoaffinity chromatography from rat brain membranes, binds to basic FGF. The protein has a large luminal domain composed of an initial Proline-Glutamine-rich segment, encoded by an uninterrupted exonic sequence of several CAG-CAA repeats. Expansion of CAG repeats has been implicated in the etiology of several neurodegenerative diseases. The Proline-Glutamine-rich segment is followed by 16 cysteine-rich repeats that contain five potential Asparagine-linked glycosylation sites, which are conserved in the human, rat, mouse, and chicken. The large extracellular domain of the protein is followed by a single transmembrane domain and a 13-amino-acid cytoplasmic carboxy-terminal tail, which is identical to that in the chicken, rat, and mouse. It is expressed in both Golgi and/or the cell membrane of multiple cell typs, including liver stellate cells, neurons, cardiac myocytes, monocytes and bronchial epithelial cells. In the blood, GLG1/ESL-1 collaborates with PSGL-1 to mediate leukocyte binding to endothelial cell surfaces

457.12 €

102-PA48S

Anti-Human ESL-1 Antibody

339 €

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