SIRPG Human

Signal-Regulatory Protein Gamma Human Recombinant
Cat. No.
BT27537
Source
Escherichia Coli.
Synonyms
signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 80.0% 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

SIRPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (29-360 a.a.) and having a molecular mass of 39.1kDa.
SIRPG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Signal-Regulatory Protein Gamma, also known as SIRPG, is a transmembrane glycoprotein belonging to the signal-regulatory protein (SIRP) family. SIRPs are known to negatively regulate signaling pathways associated with receptor tyrosine kinases. Notably, SIRPG is classified as a member of the immunoglobulin superfamily.
Description
Recombinant human SIRPG, expressed in E. coli, is available as a non-glycosylated polypeptide chain comprising 355 amino acids (specifically, residues 29-360). This protein variant has a molecular weight of 39.1 kDa. For purification and detection purposes, a 23 amino acid His-tag is fused to the N-terminus of the SIRPG protein. Purification is carried out using proprietary chromatographic methods.
Physical Appearance
The product is a clear, colorless solution that has been sterilized by filtration.
Formulation
The SIRPG protein is supplied in a solution containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea, and 10% glycerol, at a concentration of 1mg/ml.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, freezing at -20°C is recommended. The addition of a carrier protein (either 0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing of the product should be avoided.
Purity
Analysis by SDS-PAGE confirms a purity level exceeding 80.0%.
Synonyms
signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEEELQMI QPEKLLLVTV GKTATLHCTV TSLLPVGPVL WFRGVGPGRE LIYNQKEGHF PRVTTVSDLT KRNNMDFSIR ISSITPADVG TYYCVKFRKG SPENVEFKSG PGTEMALGAK PSAPVVLGPA ARTTPEHTVS FTCESHGFSP RDITLKWFKN GNELSDFQTN VDPTGQSVAY SIRSTARVVL DPWDVRSQVI CEVAHVTLQG DPLRGTANLS EAIRVPPTLE VTQQPMRVGN QVNVTCQVRK FYPQSLQLTW SENGNVCQRE TASTLTENKD GTYNWTSWFL VNISDQRDDV VLTCQVKHDG QLAVSKRLAL EVTVHQKDQS SDATP.

Product Science Overview

Introduction

Signal-Regulatory Protein Gamma (SIRPγ) is a member of the signal-regulatory protein (SIRP) family, which belongs to the immunoglobulin superfamily. SIRPγ is a type I transmembrane glycoprotein that plays a crucial role in the regulation of immune responses. It is uniquely expressed on T lymphocytes and is involved in the integrin-independent adhesion of lymphocytes to antigen-presenting cells .

Preparation Methods

The preparation of human recombinant SIRPγ typically involves the expression of the protein in a suitable host system, such as Escherichia coli (E. coli). The gene encoding SIRPγ is cloned into an expression vector, which is then introduced into the host cells. The host cells are cultured under conditions that promote the expression of the recombinant protein. After sufficient expression, the cells are harvested, and the protein is purified using techniques such as affinity chromatography .

Chemical Reactions Analysis

SIRPγ interacts with its physiological ligand, CD47, which is also known as the “don’t eat me” signal. This interaction mediates cell-cell adhesion and plays a role in the modulation of immune responses. The binding of SIRPγ to CD47 enhances antigen-specific T-cell proliferation and costimulates T-cell activation . The crystal structure of SIRPγ in complex with an antibody Fab fragment has been determined, revealing that the epitope for the Fab fragment is formed at the interface of the first and second domains of SIRPγ. This interaction stabilizes a conformation that favors SIRP dimer formation in the crystal structure .

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