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Gibco™ Human VAP-1 Recombinant Protein, PeproTech®

Catalog No. 150161mg
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Catalog No. Quantity
150161MG 1 mg
15016100UG 100 μg
1501610UG 10 μg
15016250UG 250 μg
150162UG 2 μg
15016500UG 500 μg
1501650UG 50 μg
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Catalog No. 150161MG Supplier Gibco™ Supplier No. 150161MG
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Recombinant Protein

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. This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

Copper amine oxidases catalyze the oxidative conversion of amines to aldehydes in the presence of copper and quinone cofactor. The product is a major protein on the adipocyte plasma membrane. It has adhesive properties and also has functional monoamine oxidase activity. A pseudogene for this gene has been discribed and is located approximately 9-kb downstream.

Specifications

Accession Number Q16853
For Use With (Application) ELISA, Functional Assay, Western Blot
Formulation protein with no preservative
Gene ID (Entrez) 8639
Molecular Weight (g/mol) 81.8 kDa
Name Human VAP-1
Quantity 1 mg
Source CHO cells
Regulatory Status RUO
Endotoxin Concentration <1 EU/ μg
Gene Alias amine oxidase, copper containing 3; amine oxidase, copper containing 3 (vascular adhesion protein 1); Aoc3; Copper amine oxidase; HPAO; Membrane primary amine oxidase; placenta copper monamine oxidase; semicarbazide-sensitive amine oxidase; SSAO; VAP1; VAP-1; Vascular adhesion protein 1; VP97
Common Name AOC3
Gene Symbol AOC3
Biological Activity Measured by its ability to produce hydrogen peroxide during the oxidation of benzylamine. The specific activity >16 pMoles/min/ug of VAP-1.
Conjugate Unconjugated
Recombinant Recombinant
Sequence GRGGDGGEPS QLPHCPSVSP SAQPWTHPGQ SQLFADLSRE ELTAVMRFLT QRLGPGLVDA AQARPSDNCV FSVELQLPPK AAALAHLDRG SPPPAREALA IVFFGRQPQP NVSELVVGPL PHPSYMRDVT VERHGGPLPY HRRPVLFQEY LDIDQMIFNR ELPQASGLLH HCCFYKHRGR NLVTMTTAPR GLQSGDRATW FGLYYNISGA GFFLHHVGLE LLVNHKALDP ARWTIQKVFY QGRYYDSLAQ LEAQFEAGLV NVVLIPDNGT GGSWSLKSPV PPGPAPPLQF YPQGPRFSVQ GSRVASSLWT FSFGLGAFSG PRIFDVRFQG ERLVYEISLQ EALAIYGGNS PAAMTTRYVD GGFGMGKYTT PLTRGVDCPY LATYVDWHFL LESQAPKTIR DAFCVFEQNQ GLPLRRHHSD LYSHYFGGLA ETVLVVRSMS TLLNYDYVWD TVFHPSGAIE IRFYATGYIS SAFLFGATGK YGNQVSEHTL GTVHTHSAHF KVDLDVAGLE NWVWAEDMVF VPMAVPWSPE HQLQRLQVTR KLLEMEEQAA FLVGSATPRY LYLASNHSNK WGHPRGYRIQ MLSFAGEPLP QNSSMARGFS WERYQLAVTQ RKEEEPSSSS VFNQNDPWAP TVDFSDFINN ETIAGKDLVA WVTAGFLHIP HAEDIPNTVT VGNGVGFFLR PYNFFDEDPS FYSADSIYFR GDQDAGACEV NPLACLPQAA ACAPDLPAFS HGGFSHN
Content And Storage -20°C
Expression System CHO cells
Form Lyophilized
Purity or Quality Grade ≥ 98% by SDS-PAGE gel and HPLC analyses.
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