GLIPR2 Human

GLI Pathogenesis-Related 2 Human Recimbinant
Cat. No.
BT12296
Source
Escherichia Coli.
Synonyms
GAPR-1, Golgi-associated plant pathogenesis-related protein 1, GAPR1, GLIPR-2, Golgi-associated PR-1 protein.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTeks 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

GLIPR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154) & having a molecular mass of 19.3 kDa.The GLIPR2 is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography techniques.

Product Specs

Introduction
GLIPR2, associated with plant pathogenesis-related (PR-1) proteins, exhibits increased expression in response to pathogen attacks. It resides within lipid-rich microdomains on the cytosolic face of the endomembrane system. Despite lacking a membrane-spanning domain, GLIPR2 strongly associates with membranes and is absent from the cytosol.
Description
Recombinant human GLIPR2, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 174 amino acids (residues 1-154) and possesses a molecular weight of 19.3 kDa. A 20-amino acid His-Tag is fused to the N-terminus of GLIPR2, which undergoes purification using standard chromatographic methods.
Physical Appearance
A clear, colorless solution that has undergone sterile filtration.
Formulation
The GLIPR2 protein solution, at a concentration of 1 mg/ml, consists of 20 mM Tris-HCl (pH 8), 1 mM DTT, 0.1 M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep GLIPR2 refrigerated at 4°C. For extended storage, freeze the protein at -20°C. It is advisable to supplement the protein with a carrier protein like 0.1% HSA or BSA for long-term storage. Repeated freezing and thawing should be avoided.
Purity
SDS-PAGE analysis indicates a purity exceeding 90.0%.
Synonyms
GAPR-1, Golgi-associated plant pathogenesis-related protein 1, GAPR1, GLIPR-2, Golgi-associated PR-1 protein.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGKSASKQFH NEVLKAHNEY RQKHGVPPLK LCKNLNREAQ QYSEALASTR ILKHSPESSR GQCGENLAWA SYDQTGKEVA DRWYSEIKNY NFQQPGFTSG TGHFTAMVWK NTKKMGVGKA SASDGSSFVV ARYFPAGNVV NEGFFEENVL PPKK.

Product Science Overview

Gene and Protein Structure

The GLIPR2 gene is located on chromosome 9 and is a protein-coding gene. The protein encoded by this gene is involved in several critical cellular functions, including protein homodimerization activity, positive regulation of the ERK1 and ERK2 cascade, and epithelial to mesenchymal transition (EMT) . The protein is primarily located in the Golgi membrane, which is essential for its function in cellular processes.

Biological Functions

GLIPR2 plays a significant role in the regulation of epithelial cell migration and EMT. EMT is a process where epithelial cells lose their cell polarity and adhesion properties, gaining migratory and invasive characteristics typical of mesenchymal stem cells. This transition is crucial in various physiological and pathological processes, including embryogenesis, wound healing, and cancer metastasis .

Clinical Significance

GLIPR2 has been studied extensively for its role in cancer. It has been found to be upregulated in several types of cancer, including hepatocellular carcinoma and renal clear cell carcinoma (ccRCC). In ccRCC, GLIPR2 is associated with cellular metastasis and the infiltration of CD8+ T cells . High expression levels of GLIPR2 in ccRCC are correlated with an unfavorable prognosis, making it a potential predictive biomarker for metastasis, immune infiltration, and prognosis .

Research and Therapeutic Potential

Recent studies have highlighted the potential of GLIPR2 as a target for immunotherapeutic interventions. The protein’s involvement in immune cell infiltration and its regulatory role in EMT make it a promising candidate for developing targeted therapies for cancer treatment . Further research is needed to fully understand the mechanisms by which GLIPR2 regulates these processes and to explore its potential in clinical applications.

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