SVIP Human

Small VCP/P97-Interacting Protein Human Recombinant
Cat. No.
BT22176
Source
Escherichia Coli.
Synonyms
Small VCP/P97-Interacting Protein, SVIP.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

SVIP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77) and having a molecular mass of 10.8 kDa.
SVIP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
The small VCP/p97-interacting protein (SVIP) is a regulatory factor in several cellular pathways, such as membrane fusion and ubiquitin-dependent protein degradation. Notably, SVIP acts as an inhibitor of the endoplasmic reticulum-associated degradation (ERAD) pathway. Conversely, SVIP overexpression leads to increased levels of the p62 protein, which enhances starvation-activated autophagy and promotes the sequestration of polyubiquitinated proteins and p62 within autophagosomes.
Description
Recombinant human SVIP, expressed in E. coli, is a non-glycosylated polypeptide chain containing 100 amino acids (residues 1-77) with a molecular weight of 10.8 kDa. This protein is purified using proprietary chromatographic techniques and features a 23 amino acid His-tag fused to the N-terminus.
Physical Appearance
A clear solution, sterilized by filtration.
Formulation
The SVIP solution is provided at a concentration of 0.25 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, 20% glycerol, and 2 mM DTT.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
Purity is determined to be greater than 85.0% by SDS-PAGE analysis.
Synonyms
Small VCP/P97-Interacting Protein, SVIP.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGLCFPC PGESAPPTPD LEEKRAKLAE AAERRQKEAA SRGILDVQSV QEKRKKKEKI EKQIATSGPP PEGGLRWTVS.

Product Science Overview

Introduction

Small VCP/P97-Interacting Protein (SVIP) is a crucial adaptor protein localized on the cytosolic surface of the endoplasmic reticulum (ER) membrane. It plays a significant role in the endoplasmic reticulum-associated degradation (ERAD) pathway by inhibiting the activity of p97/VCP, a protein involved in various cellular processes such as cell cycle regulation, post-mitotic membrane fusion, and ubiquitination of misfolded proteins .

Structure and Localization

SVIP is characterized by its ability to directly interact with p97/VCP. It is predominantly found on the cytosolic surface of the ER membrane, where it exerts its inhibitory effects on p97/VCP. This interaction is crucial for maintaining the balance of protein degradation within the ER, ensuring that misfolded proteins are properly managed .

Biological Functions

SVIP has been identified as an androgen-responsive gene, indicating its regulation by androgens. It plays a pivotal role in the ERAD pathway, which is responsible for the degradation of misfolded proteins within the ER. By inhibiting p97/VCP, SVIP helps regulate the degradation process, preventing the accumulation of misfolded proteins that could otherwise lead to cellular stress and dysfunction .

Role in Steroidogenesis

Recent studies have highlighted the involvement of SVIP in steroidogenesis, particularly in Leydig cells. Leydig cells are responsible for the production of testosterone, a process that involves several key proteins such as StAR, CYP17A1, and 3β-HSD. Research has shown that SVIP, along with p97/VCP, colocalizes with these proteins in Leydig cells, suggesting a regulatory role in steroidogenesis .

Experimental Findings

Experimental studies using Leydig cell lines (HLC, TM3, and MA-10) have demonstrated that the suppression of SVIP and p97/VCP using siRNAs leads to a decrease in the expression of StAR, CYP17A1, and 3β-HSD. This suppression also results in reduced testosterone levels, indicating that SVIP and p97/VCP are essential for the proper synthesis of testosterone. Additionally, it was observed that SVIP expression increases in response to hCG stimulation, further supporting its role in steroidogenesis .

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