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Manufactured by BioVendor

VAP-1 Human Chinese Hamster Ovary Cells (CHO)

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:Chinese Hamster Ovary Cells (CHO)
  • Other names:Vascular adhesion protein 1, copper-containing 3 , Voltage-dependent anion channel, VDAC
  • Species:Human
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Cat. No. Size Price

RBG10338002 2 µg
RBG10338010 10 µg
RBG10338100 100 μg
PubMed Product Details
Technical Data


Recombinant protein


VAP-1 is a type II membrane cell adhesion protein belonging to the copper/topaquinone oxidase family. It is primarily expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. VAP-1 can catalyze the oxidative deamination of low molecular weight amines, and plays an important role in the migration of lymphocytes to inflamed tissue. Inhibition of VAP-1 can protect against inflammation-related damage to certain injured tissues. Additionally, VAP-1 can function as a significant prognostic marker for certain cancers and cardiovascular diseases. Recombinant Human VAP-1 is a mixture of monomeric and disulfide-linked homodimeric forms of a 737 amino acid polypeptide, corresponding to amino acids 27 to 763 of the VAP-1 precursor. The calculated molecular weight of Recombinant Human VAP-1 is 81.8 kDa.

Amino Acid Sequence



Chinese Hamster Ovary Cells (CHO)


> 95% by SDS-PAGE gel and HPLC analysis

Biological Activity

Measured by its ability to produce hydrogen peroxide during the oxidation of benzylamine. The specific activity >16 pMoles/min/µg of VAP-1.


Endotoxin level is <0.1 ng/μg of protein (<1EU/μg).


Sterile filtred through a 0.2μm. Lyophilized from 10mM Sodium Phosphate, pH 7.8


Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1–1.0 mg/ml. Do not vortex. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at –20°C to –80°C.



Quality Control Test

Verified by UV Spectroscopy and/or SDS-PAGE gel.


This product is intended for research use only.


Research topic

Cell adhesion proteins, Oncology


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.

Summary References (16)

References to VAP-1

  • Arvilommi AM, Salmi M, Jalkanen S. Organ-selective regulation of vascular adhesion protein-1 expression in man. Eur J Immunol. 1997 Jul;27 (7):1794-800
  • Jalkanen S, Salmi M. A novel endothelial cell molecule mediating lymphocyte binding in humans. Behring Inst Mitt. 1993 Aug; (92):36-43
  • Jalkanen S, Salmi M. Vascular adhesion protein-1 (VAP-1)--a new adhesion molecule recruiting lymphocytes to sites of inflammation. Res Immunol. 1993 Nov-Dec;144 (9):746-9; discussion 754-62
  • Johansson EL, Rudin A, Wassen L, Holmgren J. Distribution of lymphocytes and adhesion molecules in human cervix and vagina. Immunology. 1999 Feb;96 (2):272-7
  • Kurkijarvi R, Adams DH, Leino R, Mottonen T, Jalkanen S, Salmi M. Circulating form of human vascular adhesion protein-1 (VAP-1): increased serum levels in inflammatory liver diseases. J Immunol. 1998 Aug 1;161 (3):1549-57
  • McNab G, Reeves JL, Salmi M, Hubscher S, Jalkanen S, Adams DH. Vascular adhesion protein 1 mediates binding of T cells to human hepatic endothelium. Gastroenterology. 1996 Feb;110 (2):522-8
  • Salmi M, Hellman J, Jalkanen S. The role of two distinct endothelial molecules, vascular adhesion protein-1 and peripheral lymph node addressin, in the binding of lymphocyte subsets to human lymph nodes. J Immunol. 1998 Jun 1;160 (11):5629-36
  • Salmi M, Jalkanen S. A 90-kilodalton endothelial cell molecule mediating lymphocyte binding in humans. Science. 1992 Sep 4;257 (5075):1407-9
  • Salmi M, Jalkanen S. Different forms of human vascular adhesion protein-1 (VAP-1) in blood vessels in vivo and in cultured endothelial cells: implications for lymphocyte-endothelial cell adhesion models. Eur J Immunol. 1995 Oct;25 (10):2803-12
  • Salmi M, Jalkanen S. Human vascular adhesion protein 1 (VAP-1) is a unique sialoglycoprotein that mediates carbohydrate-dependent binding of lymphocytes to endothelial cells. J Exp Med. 1996 Feb 1;183 (2):569-79
  • Salmi M, Kalimo K, Jalkanen S. Induction and function of vascular adhesion protein-1 at sites of inflammation. J Exp Med. 1993 Dec 1;178 (6):2255-60
  • Salmi M, Rajala P, Jalkanen S. Homing of mucosal leukocytes to joints. Distinct endothelial ligands in synovium mediate leukocyte-subtype specific adhesion. J Clin Invest. 1997 May 1;99 (9):2165-72
  • Salmi M, Tohka S, Berg EL, Butcher EC, Jalkanen S. Vascular adhesion protein 1 (VAP-1) mediates lymphocyte subtype-specific, selectin-independent recognition of vascular endothelium in human lymph nodes. J Exp Med. 1997 Aug 18;186 (4):589-600
  • Salminen TA, Smith DJ, Jalkanen S, Johnson MS. Structural model of the catalytic domain of an enzyme with cell adhesion activity: human vascular adhesion protein-1 (HVAP-1) D4 domain is an amine oxidase. Protein Eng. 1998 Dec;11 (12):1195-204
  • Smith DJ, Salmi M, Bono P, Hellman J, Leu T, Jalkanen S. Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J Exp Med. 1998 Jul 6;188 (1):17-27
  • Yoong KF, McNab G, Hubscher SG, Adams DH. Vascular adhesion protein-1 and ICAM-1 support the adhesion of tumor-infiltrating lymphocytes to tumor endothelium in human hepatocellular carcinoma. J Immunol. 1998 Apr 15;160 (8):3978-88
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