STYX Human

Serine/Threonine/Tyrosine Interacting Protein Human Recombinant
Cat. No.
BT26900
Source
E.coli.
Synonyms
Serine/threonine/tyrosine-interacting protein, Protein tyrosine phosphatase-like protein, STYX, FLJ42934.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% 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

STYX Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (1-223) and having a molecular mass of 28kDa.
STYX is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Serine/threonine/tyrosine-interacting protein (STYX), a member of the protein-tyrosine phosphatase family, is notable for its lack of catalytic activity as a phosphatase. This is due to the presence of a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop. Despite this, STYX retains the ability to bind phosphorylated substrates, potentially shielding them from phosphatases. This suggests a role in spermiogenesis. STYX is considered a potential pseudophosphatase.
Description
Recombinant human STYX, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 247 amino acids (1-223) and has a molecular mass of 28kDa. The protein is fused to a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterile-filtered.
Formulation
The STYX solution is provided at a concentration of 0.25mg/ml in a buffer consisting of 20mM Tris-HCl (pH 8.0), 30% glycerol, 1mM DTT, and 0.1M NaCl.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is greater than 85% as determined by SDS-PAGE analysis.
Synonyms
Serine/threonine/tyrosine-interacting protein, Protein tyrosine phosphatase-like protein, STYX, FLJ42934.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMEDVKL EFPSLPQCKE DAEEWTYPMR REMQEILPGL FLGPYSSAMK SKLPVLQKHG ITHIICIRQN IEANFIKPNF QQLFRYLVLD IADNPVENII RFFPMTKEFI DGSLQMGGKV LVHGNAGISR SAAFVIAYIM ETFGMKYRDA FAYVQERRFC
INPNAGFVHQ LQEYEAIYLA KLTIQMMSPL QIERSLSVHS GTTGSLKRTH EEEDDFGTMQ VATAQNG.

Product Science Overview

Introduction

Serine/Threonine/Tyrosine Interacting Protein (STYIP) is a multifunctional protein that plays a crucial role in various cellular processes. It is involved in the regulation of cell signaling pathways, particularly those related to phosphorylation, which is a key mechanism for controlling protein activity and function. The human recombinant form of this protein is produced through recombinant DNA technology, allowing for its use in research and therapeutic applications.

Structure and Function

STYIP is characterized by its ability to interact with serine, threonine, and tyrosine residues on target proteins. This interaction is essential for the regulation of protein phosphorylation, a process that involves the addition or removal of phosphate groups to or from proteins. Phosphorylation can activate or deactivate proteins, thereby influencing various cellular activities such as cell growth, differentiation, and apoptosis.

Preparation Methods

The production of human recombinant STYIP involves several steps:

  1. Gene Cloning: The gene encoding STYIP is cloned into an expression vector, which is a DNA molecule used to introduce the gene into host cells.
  2. Transformation: The expression vector is introduced into host cells, typically bacteria or yeast, through a process called transformation.
  3. Protein Expression: The host cells are cultured under conditions that promote the expression of the STYIP gene, leading to the production of the protein.
  4. Purification: The recombinant protein is purified from the host cells using techniques such as affinity chromatography, which isolates the protein based on its specific binding properties.
Chemical Reactions and Analysis

STYIP is involved in various chemical reactions related to protein phosphorylation. It acts as a kinase, transferring phosphate groups from ATP to specific serine, threonine, or tyrosine residues on target proteins. This phosphorylation can alter the activity, localization, and stability of the target proteins, thereby modulating cellular signaling pathways.

Applications

The human recombinant form of STYIP is widely used in research to study the mechanisms of protein phosphorylation and its role in cellular processes. It is also used in drug development to identify potential therapeutic targets for diseases related to dysregulated phosphorylation, such as cancer and neurodegenerative disorders.

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STYX Human (26-223)
Serine/Threonine/Tyrosine Interacting Protein (26-223 a.a.) Human Recombinant
Cat. No.
BT26980
Source
E.coli.
THE BIOTEK
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