STUB1 Human

STIP1 Homology and U-Box Containing Protein 1 Human Recombinant
Cat. No.
BT19460
Source
Escherichia Coli.
Synonyms
CHIP, UBOX1, HSPABP2, NY-CO-7, SDCCAG7, STUB1, STIP1 homology and U box-containing protein 1, Carboxy terminus of Hsp70-interacting protein, E3 ubiquitin-protein ligase CHIP, CLL-associated antigen KW-8, Antigen NY-CO-7.
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.
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Description

STUB1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids and having a molecular mass of 34.8 kDa.
STUB1 is expressed and purified by proprietary chromatographic techniques.

Product Specs

Introduction
STUB1, a highly conserved cytoplasmic protein, plays a crucial role in protein quality control. Its TPR domain facilitates interactions with chaperones Hsc70-Hsp70 and Hsp90, while its U-box domain exhibits E3 ubiquitin ligase activity. This interaction with chaperones leads to client substrate ubiquitylation and subsequent proteasomal degradation. Thus, STUB1 promotes protein degradation, linking chaperone-mediated folding with degradation pathways. Notably, STUB1 inhibits anchorage-independent cell growth and metastasis by degrading oncogenic proteins like SRC-3. Additionally, quercetin-induced inhibition of Her-2/neu tyrosine kinase activity alters Her-2/neu structure, promoting STUB1 recruitment and downregulation. STUB1 also targets and mediates the degradation of toxic, oligomeric forms of alphaSyn.
Description
Recombinant human STUB1, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 303 amino acids. With a molecular weight of 34.8 kDa, it is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The STUB1 protein solution is supplied in a buffer of 20mM Tris-HCl at pH 7.5, supplemented with 10% glycerol and 5mM DTT.
Stability
For short-term storage (up to 4 weeks), keep the vial refrigerated at 4°C. For extended storage, freeze the protein at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of STUB1 is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
CHIP, UBOX1, HSPABP2, NY-CO-7, SDCCAG7, STUB1, STIP1 homology and U box-containing protein 1, Carboxy terminus of Hsp70-interacting protein, E3 ubiquitin-protein ligase CHIP, CLL-associated antigen KW-8, Antigen NY-CO-7.
Source
Escherichia Coli.
Amino Acid Sequence
MKGKEEKEGG ARLGAGGGSP EKSPSAQELK EQGNRLFVGR KYPEAAACYG RAITRNPLVA VYYTNRALCY LKMQQHEQAL ADCRRALELD GQSVKAHFFL GQCQLEMESY DEAIANLQRA YSLAKEQRLN FGDDIPSALR IAKKKRWNSI EERRIHQESE LHSYLSRLIA AERERELEEC QRNHEGDEDD SHVRAQQACI EAKHDKYMAD MDELFSQVDE KRKKRDIPDY LCGKISFELM REPCITPSGI TYDRKDIEEH LQRVGHFDPV TRSPLTQEQL IPNLAMKEVI DAFISENGWV EDY.

Product Science Overview

Introduction

STIP1 Homology and U-Box Containing Protein 1, also known as STUB1, is a protein encoded by the STUB1 gene located on chromosome 16q13.3. This protein is also referred to as CHIP (C-terminus of Hsc70-Interacting Protein). It plays a crucial role in protein quality control and is involved in various physiological and pathological processes, including neurodegenerative diseases, cancer, and immune responses .

Structure

STUB1/CHIP is characterized by three distinct domains:

  1. Amino-terminal Tetratricopeptide Repeat (TPR) Domain: This domain is involved in protein-protein interactions, particularly with molecular chaperones such as Hsp70 and Hsp90.
  2. Highly Charged Middle Domain: This domain is essential for the structural integrity of the protein.
  3. Carboxy-terminal U-box Domain: This domain confers E3 ubiquitin ligase activity, enabling the protein to tag misfolded proteins for degradation via the ubiquitin-proteasome system .
Function

STUB1/CHIP is a molecular chaperone-associated E3 ubiquitin ligase. It is involved in the regulation of protein quality control by promoting the degradation of misfolded or damaged proteins. This function is critical for maintaining cellular homeostasis and preventing the accumulation of toxic protein aggregates that can lead to diseases .

Clinical Significance

Mutations in the STUB1 gene have been associated with various forms of spinocerebellar ataxia, including autosomal recessive cerebellar ataxia 16 (SCAR16) and spinocerebellar ataxia 48 (SCA48). These conditions are characterized by progressive cerebellar ataxia, cognitive decline, dystonia, parkinsonism, and other neurological symptoms. The age of onset and severity of symptoms can vary widely among individuals .

Research and Therapeutic Potential

Recent studies have highlighted the potential of targeting STUB1/CHIP in therapeutic strategies for neurodegenerative diseases and cancer. By modulating its activity, it may be possible to enhance the degradation of pathogenic proteins and improve cellular function. Additionally, understanding the molecular mechanisms underlying STUB1-related disorders can provide insights into the development of novel treatments .

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