VBP1 Human

Von Hippel-Lindau Binding Protein 1 Human Recombinant
Cat. No.
BT6196
Source
Escherichia Coli.
Synonyms
Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

VBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197 a.a) and having a molecular mass of 25kDa.
VBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Prefoldin subunit 3 (VBP1), a member of the prefoldin subunit alpha family, interacts with the Von Hippel-Lindau protein to form an intracellular complex. As a chaperone protein, VBP1 is believed to play a role in transporting the Von Hippel-Lindau protein from perinuclear granules to either the nucleus or the cytoplasm. VBP1 exhibits specific binding to cytosolic chaperonin (c-CPN), facilitating the transfer of target proteins. Additionally, VBP1 binds to nascent polypeptide chains, promoting folding in environments with multiple competing pathways for nonnative proteins.
Description
Recombinant human VBP1, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 220 amino acids (residues 1-197) and has a molecular weight of 25 kDa. The protein includes a 23-amino acid His-tag fused at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Sterile, colorless solution.
Formulation
The VBP1 protein solution is provided at a concentration of 0.5 mg/ml. The solution contains 20 mM Tris-HCl buffer (pH 8.0), 0.2 M NaCl, 50% glycerol, and 2 mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure long-term stability during storage, adding a carrier protein (0.1% HSA or BSA) is advisable. Repeated freezing and thawing should be avoided.
Purity
The purity of the protein is greater than 90.0% as determined by SDS-PAGE analysis.
Synonyms
Prefoldin subunit 3, HIBBJ46, Von Hippel-Lindau-binding protein 1, VBP-1, VHL-binding protein 1, VBP1, PFDN3, PFD3.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAAVKDS CGKGEMATGN GRRLHLGIPE AVFVEDVDSF MKQPGNETAD TVLKKLDEQY QKYKFMELNL AQKKRRLKGQ IPEIKQTLEI LKYMQKKKES TNSMETRFLL ADNLYCKASV PPTDKVCLWL GANVMLEYDI DEAQALLEKN LSTATKNLDS LEEDLDFLRD QFTTTEVNMA RVYNWDVKRR NKDDSTKNKA.

Product Science Overview

Introduction

Von Hippel-Lindau Binding Protein 1 (VBP1) is a crucial protein that interacts with the Von Hippel-Lindau (VHL) tumor suppressor protein. This interaction is significant in the regulation of various cellular processes, including transcriptional elongation and protein transport. The recombinant form of VBP1, produced through genetic engineering techniques, is widely used in research to study its functions and interactions.

Structure and Function

VBP1 belongs to the prefoldin subunit alpha family and functions as a chaperone protein. It assists in the proper folding and stabilization of other proteins, particularly the VHL protein. VBP1 is believed to play a role in the transport of the VHL protein from the perinuclear granules to the nucleus or cytoplasm .

Interaction with VHL Protein

The VHL protein is involved in the down-regulation of transcriptional elongation by preventing the association of elongin B and C with the catalytic subunit elongin A. Mutations in the VHL gene lead to Von Hippel-Lindau disease, characterized by various neoplasias, including hemangioblastomas, renal cell carcinomas, and pheochromocytomas . VBP1 binds to the VHL protein, forming an intracellular complex that is essential for the proper functioning of the VHL protein .

Expression and Localization

Studies have shown that VBP1 is ubiquitously expressed in various tissues. In fetal stages, it is primarily expressed in the central nervous system, retina, and liver. In adult tissues, VBP1 expression is widespread, with specific cell types in the brain, eye, kidney, and intestine showing higher levels of expression . The gene encoding VBP1 is located in a region homologous to human Xq28 .

Recombinant VBP1

Recombinant human VBP1 is produced using E. coli expression systems. The recombinant protein typically includes an N-terminal His-tag to facilitate purification. It is used in various research applications to study the protein’s structure, function, and interactions. The recombinant VBP1 protein is purified using conventional chromatography techniques and is available in high purity for research purposes .

Applications in Research

Recombinant VBP1 is a valuable tool in molecular biology and biomedical research. It is used to investigate the mechanisms of VHL-related diseases, study protein-protein interactions, and explore the role of chaperone proteins in cellular processes. Understanding the function and regulation of VBP1 can provide insights into the development of therapeutic strategies for diseases associated with VHL mutations .

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