VAP-1 Recombinant Protein | 40-576

VAP-1 Recombinant Protein | 40-576 | Gentaur UK, US & Europe Distribution

Tested Application: N/A

Application: N/A

Tpredicted Molecular Weight: N/A

Physical State: Lyophilized

Buffer: N/A

Storage Condition: The lyophilized VAP-1 recombinant protein is stable for at least 2 years from date of receipt at -20˚C. Reconstituted VAP-1 stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚C. As with any protein, exposing VAP-1 recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.

Alternate Name: HPAO, SSAO, VAP1, VAP-1, Membrane primary amine oxidase, Copper amine oxidase

Background: N/A

Shipping: N/A

Disclaimer: This product is for research use only.

Source: CHO cells

Species: Human

By Source: CHO Cells

By Species: Human

Fusion Tag: N/A

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

Bological Activity: Biological activity was 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 less than 0.1 ng per μg of VAP-1 (1EU/μg).

Purity: Greater than 95% by SDS-PAGE gel and HPLC analyses.