SH3BGRL Human

SH3 Domain Binding Glutamic Acid-Rich Protein Like Human Recombinant
Cat. No.
BT25553
Source
Escherichia Coli.
Synonyms
SH3 domain-binding glutamic acid-rich-like protein, SH3BGRL, SH3BGR.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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

SH3BGRL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-114 a.a) and having a molecular mass of 15.3kDa.
SH3BGRL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
SH3 domain-binding glutamic acid-rich-like protein (SH3BGRL) is a member of the human SH3BGR family. Located on chromosome Xq13.3, the SH3BGRL gene encodes a small, 114-amino acid protein widely found in tissues like the liver and blood. SH3BGRL protein features a proline-rich sequence (PLPPQIF) encompassing both the SH3 binding (PXXP)3 and the Homer EVH1 binding (PPXXF)4 motifs.
Description
Recombinant SH3BGRL Human, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 138 amino acids (1-114 a.a). It possesses a molecular mass of 15.3 kDa. The protein includes a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The SH3BGRL protein solution is provided at a concentration of 1 mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 10% glycerol, and 0.15M NaCl.
Stability
For short-term storage (2-4 weeks), the product can be kept at 4°C. For extended storage, freezing at -20°C is recommended. The addition of a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the SH3BGRL protein is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
SH3 domain-binding glutamic acid-rich-like protein, SH3BGRL, SH3BGR.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMVIRVY IASSSGSTAI KKKQQDVLGF LEANKIGFEE KDIAANEENR KWMRENVPEN SRPATGYPLP PQIFNESQYR GDYDAFFEAR ENNAVYAFLG LTAPPGSKEA EVQAKQQA.

Product Science Overview

Introduction

The SH3 Domain Binding Glutamic Acid-Rich Protein Like (SH3BGRL) is a member of a small family of proteins that are characterized by their ability to bind to SH3 domains. These proteins are involved in various cellular processes, including signal transduction, cytoskeletal organization, and cellular migration. The human recombinant form of SH3BGRL has been studied for its potential roles in cancer and other diseases.

Gene and Protein Structure

The SH3BGRL gene is located on human chromosome 1 at the position 1p36.11 . The gene encodes a protein that is approximately 10.5 kDa in size and has an isoelectric point of 5.0 . The SH3BGRL protein family includes several homologous proteins, such as SH3BGR, SH3BGRL, and SH3BGRL3, which are located on different chromosomes and have varying expression patterns .

Expression and Localization

SH3BGRL is ubiquitously expressed in human tissues, with higher expression levels observed in certain tissues such as the spleen, thymus, and various arteries . The protein is found in multiple cellular compartments, including the nucleus, cytoplasm, and extracellular exosomes . This widespread expression suggests that SH3BGRL may play a fundamental role in various cellular functions.

Biological Functions

While the precise functions of SH3BGRL are not fully understood, it is known to be involved in redox homeostasis and electron transport chain processes . The protein shows significant similarity to glutaredoxin 1 of E. coli, which is an oxidoreductase involved in reducing intracellular protein disulfides . However, SH3BGRL lacks the enzymatic activity of glutaredoxins and may instead act as a regulator of redox activity .

Role in Cancer

SH3BGRL has been implicated in cancer, particularly in glioblastoma multiforme, where it is up-regulated compared to normal cerebral tissue . The protein has also been found to be overexpressed in several other tumors, suggesting a potential role in tumorigenesis . Recent studies have indicated that SH3BGRL may interact with members of the EGFR family, which are known to be involved in cancer progression .

Molecular Interactions

SH3BGRL interacts with myosin 1c in a calcium-dependent manner, which modulates cellular migration . This interaction is crucial for the regulation of cytoskeletal dynamics and cell motility. The binding of SH3BGRL to myosin 1c requires the presence of calcium, suggesting that calcium-driven mechanisms may regulate the conformation and activity of myosin 1c .

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