sVAP-1 Human ELISA
| Other names: Vascular adhesion protein 1, Membrane copper amine oxidase, Semicarbazide-sensitive amine oxidase, Amine oxidase,copper-containing,3, Diamine oxidase, Histaminase | Product of BioVendor | ||||
| Product: | Size: | ||||
|---|---|---|---|---|---|
| RBMS259R (regulatory status: RUO) | 96 wells (1 kit) | ||||
Files:
Datasheet PDF (RUO)MSDS (RUO)
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Product details
Summary
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.
Research topic
Cell adhesion proteins
Assay format
Sandwich ELISA, Biotin-labelled antibody
Applications
Amniotic fluid, Cell culture supernatant, Plasma-EDTA, Plasma-Heparin, Serum
Sample requirements
10 µl (1:100 prediluted)
Storage/Shipping
Store kit reagents between 2 – 8°C.
Calibration Curve
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Calibration range
31.3 – 2000 pg/ml
Limit of detection
19 pg/ml
Intra-assay
CV = 3.0%
Inter-assay
CV = 4.5%
Spiking Recovery
96%
Dilution Linearity
89%
References to summary
- Holmgren J, Johansson EL, Rudin A, Wassen L. Distribution of lymphocytes and adhesion molecules in human cervix and vagina. Immunology. 1999 Feb;96 (2):272-7
- Jalkanen S, Arvilommi AM, Salmi M. 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
- 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, Kurkijarvi R, Adams DH, Leino R, Mottonen T, Jalkanen S. 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
- 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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