CSK Human

C-Src Tyrosine Kinase Human Recombinant
Cat. No.
BT9645
Source
Escherichia Coli.
Synonyms
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec'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

CSK Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-450) and having a molecular mass of 53.1 kDa.
The CSK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
C-Src Tyrosine Kinase, also called CSK, is a crucial player in regulating various cellular processes such as growth, movement, specialization, and immune responses. Its primary role is to phosphorylate tyrosine residues within the C-terminal tails of Src-family kinases. The CSK gene encodes a protein that acts as a suppressor of signaling pathways initiated by multiple cell surface receptors. Notably, CSK is implicated in pathways like the PI-3K cascade and signaling by FGFR.
Description
Recombinant human CSK, expressed in E. coli, is a single polypeptide chain devoid of glycosylation. It comprises 473 amino acids (specifically residues 1-450) and exhibits a molecular weight of 53.1 kDa. This CSK variant features a 23 amino acid His-Tag fused at its N-terminus, facilitating purification through specialized chromatographic methods.
Physical Appearance
A clear solution that has undergone sterile filtration.
Formulation
The CSK protein solution has a concentration of 0.5 mg/ml and is prepared in a buffer containing Phosphate Buffered Saline (pH 7.4), 20% glycerol, and 1mM DTT.
Stability
For short-term storage (up to 2-4 weeks), maintain the product at 4°C. For extended storage, freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage to preserve protein integrity. It's crucial to minimize repeated cycles of freezing and thawing.
Purity
SDS-PAGE analysis confirms a purity exceeding 95.0%.
Synonyms
Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSAIQAA WPSGTECIAK YNFHGTAEQD LPFCKGDVLT IVAVTKDPNW YKAKNKVGRE GIIPANYVQK REGVKAGTKL SLMPWFHGKI TREQAERLLY PPETGLFLVR ESTNYPGDYT LCVSCDGKVE HYRIMYHASK LSIDEEVYFE NLMQLVEHYT SDADGLCTRL IKPKVMEGTV AAQDEFYRSG WALNMKELKL LQTIGKGEFG DVMLGDYRGN KVAVKCIKND ATAQAFLAEA SVMTQLRHSN LVQLLGVIVE EKGGLYIVTE YMAKGSLVDY LRSRGRSVLG GDCLLKFSLD VCEAMEYLEG NNFVHRDLAA RNVLVSEDNV AKVSDFGLTK EASSTQDTGK LPVKWTAPEA LREKKFSTKS DVWSFGILLW EIYSFGRVPY PRIPLKDVVP RVEKGYKMDA PDGCPPAVYE VMKNCWHLDA AMRPSFLQLR EQLEHIKTHE LHL.

Product Science Overview

Introduction

C-Src Tyrosine Kinase, also known as CSK, is a non-receptor tyrosine kinase that plays a crucial role in regulating various cellular processes, including cell growth, migration, differentiation, and immune response . It is a member of the Src family kinases (SFKs), which are involved in signaling pathways that control these cellular functions.

Structure and Function

C-Src Tyrosine Kinase is composed of several key domains:

  • SH2 Domain: This domain binds to phosphorylated tyrosine residues on other proteins, facilitating protein-protein interactions.
  • SH3 Domain: This domain binds to proline-rich sequences in other proteins, further aiding in protein interactions.
  • Kinase Domain: This domain is responsible for the enzyme’s catalytic activity, transferring phosphate groups to tyrosine residues on substrate proteins.

The primary function of C-Src is to phosphorylate tyrosine residues located in the C-terminal tails of Src-family kinases, which regulates their activity . This phosphorylation event stabilizes SFKs in a closed, inactive conformation by engaging the SH2 domain in cis .

Biological Activity

Recombinant human active C-Src is produced in Sf9 cells and purified via sequential chromatography . It has a molecular weight of approximately 60 kDa and a purity of 95% as determined by SDS-PAGE analysis . The biological activity of C-Src is measured by its ability to transfer phosphate groups to specific peptide substrates, with an activity of approximately 290 units/mg .

Regulatory Mechanisms

C-Src activity is tightly regulated by several mechanisms:

  1. Phosphorylation: Phosphorylation of the C-terminal tail tyrosine by C-terminal Src kinase (Csk) stabilizes SFKs in an inactive conformation .
  2. Protein-Protein Interactions: Binding of the SH2 and SH3 domains to specific sequences in other proteins modulates C-Src activity.
  3. Non-Catalytic Inhibition: Csk and Csk-homologous kinase (Chk) can inhibit SFKs through non-catalytic mechanisms, involving direct binding to active forms of SFKs .
Applications

Recombinant C-Src Tyrosine Kinase is widely used in research to study signal transduction pathways, cancer biology, and the development of targeted therapies. Its role in regulating cell growth and differentiation makes it a valuable tool for understanding various diseases and developing new treatments.

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