> >Chaperone SURA E.Coli Recombinant ( SURA E.Coli )
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Chaperone SURA E.Coli Recombinant ( SURA E.Coli )

DescriptionSURA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 429 amino acids (21-428 a.a.) and having a molecular weight of 47.3kDa. The SURA is fused to 20 a.a His-Tag at N-terminus and purified by

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Data sheet

Formulation The SURA 1mg/ml protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.
Purity Greater than 95.0% as determined by SDS-PAGE.
Description SURA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 429 amino acids (21-428 a.a.) and having a molecular weight of 47.3kDa. The SURA is fused to 20 a.a His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Protein Background SURA is a PPIase enzyme and chaperone of Escherichia coli and other Gram-negative bacteria. SURA is a key player in the biogenesis of beta-barrel outer membrane proteins and is involved in cell envelope homeostasis and cell envelope functions. SURA is necessary for the survival of E.coli in stationary phase and needed for pilus biogenesis.
Expression host Escherichia Coli.
Synonyms Rotamase surA, Survival protein A.
Stability Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino acid sequence MGSSHHHHHH SSGLVPRGSH MAPQVVDKVA AVVNNGVVLE SDVDGLMQSV KLNAAQARQQ LPDDATLRHQ IMERLIMDQI ILQMGQKMGV KISDEQLDQA IANIAKQNNM TLDQMRSRLA YDGLNYNTYR NQIRKEMIIS EVRNNEVRRR ITILPQEVES LAQQVGNQND ASTELNLSHI LIPLPENPTS DQVNEAESQA RAIVDQARNG ADFGKLAIAH SADQQALNGG QMGWGRIQEL PGIFAQALST AKKGDIVGPI RSGVGFHILK VNDLRGESKN ISVTEVHARH ILLKPSPIMT DEQARVKLEQ IAADIKSGKT TFAAAAKEFS QDPGSANQGG DLGWATPDIF DPAFRDALTR LNKGQMSAPV HSSFGWHLIE LLDTRNVDKT DAAQKDRAYR MLMNRKFSEE AASWMQEQRA SAYVKILSN.
Physical Appearence Sterile filtered colorless solution.
Biological Activity Specific activity is > 450 nmoles/min/ug, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

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