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map, 1-264aa, E.coli, His tag, E.coli

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Cat# 01-P1025-500ug

Size : 500ug

Brand : American Research Products

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map, 1-264aa

Category: Proteins

Catalog

01-P1025

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Product Name	map, 1-264aa
Description	Methionine aminopeptidases, also designated peptidase M proteins, are members of the M24 family of proteins. This protein removes the amino-terminal methionine residue from nascent polypeptides. The active site of map contains two adjacent divalent metal ions connected by a water molecule or hydroxide ion. Recombinant E.coli map protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Synonyms	Methionine aminopeptidase., ECK0166, JW0163, pepM
Host	E. coli
Molecular Weight	30.5 kDa(267aa), confirmed by MALDI-TOF
Amino Acid Sequence	MGSSHHHHHH SSGLVPRGSH MAISIKTPED IEKMRVAGRL AAEVLEMIEP YVKPGVSTGE LDRICNDYIV NEQHAVSACL GYHGYPKSVC ISINEVVCHG IPDDAKLLKD GDIVNIDVTV IKDGFHGDTS KMFIVGKPTI MGERLCRITQ ESLYLALRMV KPGINLREIG AAIQKFVEAE GFSVVREYCG HGIGRGFHEE PQVLHYDSRE TNVVLKPGMT FTIEPMVNAG KKEIRTMKDG WTVKTKDRSL SAQYEHTIVV TDNGCEILTL RKDDTIPAII SHDE
Tag	His-tag
Reactivity	E. coli
Applications	SDS-PAGE
Form	Liquid, in 20mM Tris-HCl buffer (pH8.0) containing 20% glycerol, 0.1M NaCl and 1mM DTT
Concentration	1.0 mg/ml (determined by Bradford assay)
Purity	> 90% by SDS-PAGE
Storage	Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles.
References	Bernier SG., et al. (2005) J Cell Biochem. 95(6):1191-203.
Background	Methionine aminopeptidases, also designated peptidase M proteins, are members of the M24 family of proteins. This protein removes the amino-terminal methionine residue from nascent polypeptides. The active site of map contains two adjacent divalent metal ions connected by a water molecule or hydroxide ion. Recombinant E.coli map protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Supplier	ARP

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