VDAC1 Human,
Rabbit Polyclonal Antibody

Research topic

Cell adhesion proteins

Introduction to the Molecule

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.

Source of Antigen

Synthesis peptide (KLH coupled) corresponding to C-terminal residues of Human VDAC1

Host

Rabbit

Preparation

PBS containing 50% glycerol

Species Reactivity

Human (+), Mouse (+), Rat (+)

Storage/Stability

store for 1 year at –20°C from date of shipment

Applications

Western blotting

By research topic:

• Cell adhesion proteins

By molecule:

• VAP-1
• Voltage-dependent anion channel