STAC Human

SH3 And Cysteine Rich Domain Human Recombinant
Cat. No.
BT20845
Source
Escherichia Coli.
Synonyms
SH3 and cysteine rich domain, STAC, STAC1, SH3 and cysteine-rich domain-containing protein, Src homology 3 and cysteine-rich domain-containing protein.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% 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

STAC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-402 a.a.) and having a molecular mass of 46.9kDa.
STAC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
STAC (SH3 and Cysteine Rich Domain) contains a phorbol-ester/DAG-type zinc finger and an SH3 domain. It plays a role in neuron-specific signal transduction.
Description
Recombinant human STAC protein, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 425 amino acids (residues 1-402) with a molecular weight of 46.9 kDa. It includes an N-terminal 23-amino acid His-tag and is purified using proprietary chromatographic methods.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The STAC protein solution (1 mg/ml) is supplied in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.4 M Urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the protein at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for extended storage. Repeated freeze-thaw cycles should be avoided.
Purity
The purity is determined to be greater than 85% by SDS-PAGE analysis.
Synonyms
SH3 and cysteine rich domain, STAC, STAC1, SH3 and cysteine-rich domain-containing protein, Src homology 3 and cysteine-rich domain-containing protein.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMIPPSSP REDGVDGLPK EAVGAEQPPS PASTSSQESK LQKLKRSLSF KTKSLRSKSA DNFFQRTNSE DMKLQAHMVA EISPSSSPLP APGSLTSTPA RAGLHPGGKA HAFQEYIFKK PTFCDVCNHM IVGTNAKHGL RCKACKMSIH HKCTDGLAPQ RCMGKLPKGF RRYYSSPLLI HEQFGCIKEV MPIACGNKVD PVYETLRFGT SLAQRTKKGS SGSGSDSPHR TSTSDLVEVP EEANGPGGGY DLRKRSNSVF TYPENGTDDF RDPAKNINHQ GSLSKDPLQM NTYVALYKFV PQENEDLEMR PGDIITLLED SNEDWWKGKI QDRIGFFPAN FVQRLQQNEK IFRCVRTFIG CKEQGQITLK ENQICVSSEE EQDGFIRVLS GKKKGLIPLD VLENI.

Product Science Overview

Introduction

The SH3 and Cysteine Rich Domain, often abbreviated as STAC, is a protein coding gene that plays a crucial role in various cellular processes. This domain is characterized by the presence of Src Homology 3 (SH3) and cysteine-rich regions, which are essential for its function in cellular signaling and protein interactions.

Structure and Function

The SH3 domain is a small protein module consisting of approximately 60 amino acids. It is arranged in a compact β-barrel fold made up of five β-strands connected by loops and a 3_10-helix . The SH3 domain is known for its ability to mediate protein-protein interactions by binding to proline-rich motifs in partner proteins. This interaction is critical for the assembly of protein complexes involved in various biological processes, including cell survival, proliferation, differentiation, migration, and polarity .

The cysteine-rich domain, on the other hand, is involved in the regulation of protein localization and activity. It plays a significant role in the positive regulation of voltage-gated calcium channel activity and skeletal muscle contraction . The STAC gene, which encodes the SH3 and cysteine-rich domain-containing protein, is specifically expressed in skeletal muscle and is essential for muscle development and function .

Biological Significance

The SH3 and cysteine-rich domain-containing proteins are implicated in several physiological pathways and are associated with various diseases. For instance, mutations in the STAC3 gene have been linked to congenital myopathy, a condition characterized by muscle weakness and developmental delays . Additionally, the SH3 domain is involved in the development of diseases such as cancer, leukemia, osteoporosis, Alzheimer’s disease, and various infections .

Research and Applications

Research on SH3 and cysteine-rich domains has provided valuable insights into their role in cellular signaling and disease mechanisms. The ability of SH3 domains to mediate protein-protein interactions makes them potential targets for drug development. By targeting these interactions, it may be possible to develop therapies for diseases associated with SH3 domain dysfunction .

In the context of recombinant protein technology, human recombinant SH3 and cysteine-rich domain proteins are used in various research applications. These include studying protein interactions, understanding disease mechanisms, and developing potential therapeutic interventions.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.