Home  >  Products  >  melA, Recombinant, E.coli, aa1-451, His-Tag (Alpha-galactosidase, Melibiase, mel-7, b4119, JW4080)

melA, Recombinant, E.coli, aa1-451, His-Tag (Alpha-galactosidase, Melibiase, mel-7, b4119, JW4080)

Cat no: 045442


Supplier: United States Biological
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melA (alpha-galactosidase) belongs to glycosyl hydrolase 4 family. Alpha-galactosidases catalyse the hydrolysis of saccharides containing o-1,6,-galactoside linkages. The three alpha-galactosidases catalyse the same reaction, but are localized in different cellular compartments: The E.coli enzyme is cytoplasmic protein and the human enzyme and the yeast enzyme is secretory proteins. Therefore, although the active enzyme from all three species has nearly the same molecular weight, structural similarities, as well as differences, are expected. Recombinant protein corresponding to aa1-451 from E.coli melA, fused to His-tag at N-terminus, expressed in E.coli. AA Sequence: MGSSHHHHHH SSGLVPRGSH MGSMMSAPKI TFIGAGSTIF VKNILGDVFH REALKTAHIA LMDIDPTRLE ESHIVVRKLM DSAGASGKIT CHTQQKEALE DADFVVVAFQ IGGYEPCTVT DFEVCKRHGL EQTIADTLGP GGIMRALRTI PHLWQICEDM TEVCPDATML NYVNPMAMNT WAMYARYPHI KQVGLCHSVQ GTAEELARDL NIDPATLRYR CAGINHMAFY LELERKTADG SYVNLYPELL AAYEAGQAPK PNIHGNTRCQ NIVRYEMFKK LGYFVTESSE HFAEYTPWFI KPGREDLIER YKVPLDEYPK RCVEQLANWH KELEEYKKAS RIDIKPSREY ASTIMNAIWT GEPSVIYGNV RNDGLIDNLP QGCCVEVACL VDANGIQPTK VGTLPSHLAA LMQTNINVQT LLTEAILTEN RDRVYHAAMM DPHTAAVLGI DEIYALVDDL IAAHGDWLPG WLHR Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Catalogue number: 045442
Size: 50ug
Form: Supplied as a liquid in 20mM Tris-HCl, pH 8.0, 1mM DTT, 0.1M sodium chloride, 10% glycerol.
Purity: ~90% (SDS-PAGE)
References: 1. Naumov G., et al. (1990) Mol Gen Genet. 224(1):119-28. 2. Naumov G., et al. (1995) Yeast. 30(5): 481-3.

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