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SecB

目录号 : GP24515

Protein Export Protein SecB Recombinant

SecB Chemical Structure

规格 价格 库存 购买数量
5μg
¥840.00
5-10工作日
25μg
¥2,030.00
5-10工作日
1mg
¥37,800.00
5-10工作日

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Sample solution is provided at 25 µL, 10mM.

Description

Recombinant E.Coli SecB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids and having a molecular mass of 17.2 kDa. SecB was over-expressed in E. coli and purified by conventional chromatography.

Product Data

Purity Greater than 95.0% as determined by SDS-PAGE. Source Escherichia Coli.
Phycical Appearance Sterile Filtered colorless solution. Shipping Condition Shipped with Ice Packs.
Synonyms Protein-export protein secB; secB; b3609; JW3584.
Amino Acid Sequence MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA.
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.
Formulation The SecB protein solution (1mg/ml) contains 20mM Tris-HCl pH-8 and 10% glycerol.

Introduction

SecB, a significant chaperone that takes part in protein export, binds various ligands rapidly with high affinity and low specificity. SecB plays an important role during protein export through the general secretory pathway by modulating the partitioning of precursors between folding or aggregation and delivery to the membrane-bound translocation apparatus. SecB has the potential to take part in functions outside of export acting as a universal nonspecific chaperone to provide buffering capacity of the nonnative state of proteins in the cytosolic pool.

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.

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