Recombinant Human VBP1 Protein

Beta LifeScience SKU/CAT #: BL-4425PS
Recombinant Human VBP1 Protein

Recombinant Human VBP1 Protein

Beta LifeScience SKU/CAT #: BL-4425PS
Catalog No.: BL-4425PS

Product Overview

Tag N/A
Host Species Human
Synonym Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.
Background Prefoldin subunit 3 (VBP1) is a member of the prefoldin subunit alpha family. VBP1 interacts with the Von Hippel-Lindau protein in order to create an intracellular complex. Since VBP1 serves as a chaperone protein, it is assumed to have a role in the transport of the Von Hippel-Lindau protein from the perinuclear granules to the nucleus or cytoplasm. VBP1 binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. VBP1 also binds to nascent polypeptide chain and stimulates folding in an environment in which there are numerous competing pathways for nonnative proteins.
Description VBP1 Human Recombinant expressed in E.Coli is a single, non-glycosylated polypeptide chain containing 220a.a. (1-197 a.a) and having a molecular weight of 25kDa.VBP1 is fused to a 23a.a. His-tag at N-terminus and purified by unique purification methods.
Source E.coli
AA Sequence MGSSHHHHHH SSGLVPRGSH MGSMAAVKDS CGKGEMATGN GRRLHLGIPE AVFVEDVDSF MKQPGNETAD TVLKKLDEQY QKYKFMELNL AQKKRRLKGQ IPEIKQTLEI LKYMQKKKES TNSMETRFLL ADNLYCKASV PPTDKVCLWL GANVMLEYDI DEAQALLEKN LSTATKNLDS LEEDLDFLRD QFTTTEVNMA RVYNWDVKRR NKDDSTKNKA.
Purity >90.0% as determined by SDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Formulation VBP1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.
Stability Recombinant protein is stable for 12 months at -70°C
Usage For Research Use Only
Storage 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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