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VAP-1 (Vascular adhesion protein 1, copper-containing 3 )

The mature VAP-1 molecule is a 170 kDa homodimeric glycoprotein that consists of two 90 kDa subunits held together by disulfide bonds. VAP-1 has a large extracellular domain, a single-pass transmembrane domain, and a short cytoplasmic tail. The molecule has abundant sialic acid decorations that are essential to its adhesive function, because VAP-1 is unable to mediate lymphocyte adhesion to desialylated vessels. The leukocyte ligand for VAP-1 is currently unknown. Induction of VAP-1 has been shown at sites of inflam-mation, such as in inflammatory bowel diseases and chronic dermatoses, where expression of VAP-1 is clearly increased. It is constitutively expressed on hepatic endothelium playing a critical role in regulation of T-cell recirculation to the liver. Strong expression of VAP-1 on tumor endothelium distinguishes human hepatocellular carcinomas from colorectal hepatic metastases.

1 results found in Immunoassays
1 results found in Proteins.
1 results found in Antibodies.

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sVAP-1 Human ELISA

Type: Sandwich ELISA, Biotin-labelled antibody

RAF117R 96 wells (1 kit)

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VAP-1 Human Chinese Hamster Ovary Cells (CHO)

Type: Recombinant

RBG10338002 2 µg
RBG10338010 10 µg
RBG10338100 100 μg

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VDAC1 Human, Rabbit Polyclonal Antibody

LF-PA0155 100 ul
Find more on VAP-1 on pubmed

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