Human VAP-1 Protein 2643

$270.00 – $900.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Gly27-Asn763

SKU: 2643parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	Q16853
express system	HEK293
product tag	N-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	The semicarbazide-sensitive amine oxidase (SSAO), also known as vascular adhesion protein-1 (VAP-1) or primary amine oxidase (PrAO), is a deaminating enzyme highly expressed in vessels that generates harmful products as a result of its enzymatic activity. As a multifunctional enzyme, it is also involved in inflammation through its ability to bind and promote the transmigration of circulating leukocytes into inflamed tissues.
molecular weight	The protein has a predicted MW of 82.88 kDa. Due to glycosylation, the protein migrates to 100-120 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human VAP-1 Protein 2643

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
The semicarbazide-sensitive amine oxidase (SSAO), also known as vascular adhesion protein-1 (VAP-1) or primary amine oxidase (PrAO), is a deaminating enzyme highly expressed in vessels that generates harmful products as a result of its enzymatic activity. As a multifunctional enzyme, it is also involved in inflammation through its ability to bind and promote the transmigration of circulating leukocytes into inflamed tissues.
Protein names Amine oxidase [copper-containing] 3 (EC 1.4.3.21) (Amine oxidase copper-containing 3) (Copper amine oxidase) (HPAO) (Semicarbazide-sensitive amine oxidase) (SSAO) (Vascular adhesion protein 1) (VAP-1)
Gene names AOC3,AOC3 VAP1
Protein family Copper/topaquinone oxidase family
Mass 9606Da
Function Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia (PubMed:19588076, PubMed:24304424, PubMed:9653080). Has a preference for the primary monoamines methylamine and benzylamine (PubMed:19588076, PubMed:9653080). Could also act on 2-phenylethylamine but much less efficiently (PubMed:19588076). At endothelial cells surface can also function as a cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion (PubMed:9254657, PubMed:9653080).; [Isoform 2]: Has no semicarbazide-sensitive amine oxidase (SSAO) activity.
Catalytic activity #N/A
Subellular location Cell membrane ; Single-pass type II membrane protein .
Tissues Strongly expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. Also highly expressed in appendix, lung and small intestine. Expressed also in adipose tissue, in bone marrow, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, spleen and testis. Isoform 2 seems to be the predominant transcript in fetal kidneys, fetal cartilage and fetal tonsils. The highest relative expression of isoform 2 occurs in skeletal muscle, heart, pancreas, kidney, and lung.
Structure Homodimer; disulfide-linked (PubMed:16046623). Can heterodimerize with isoform 2 leading to reduced surface expression (PubMed:23349812). Probably forms heterodimers with AOC2 (PubMed:19588076).
Post-translational modification Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.; N- and O-glycosylated.
Target Relevance information above includes information from UniProt accession: Q16853
The UniProt Consortium

Data

The purity of Human VAP-1 is greater than 95% as determined by SEC-HPLC.

Human VAP-1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.