GPI Human

Glucose-6-Phosphate Isomerase Human Recombinant
Cat. No.
BT400
Source
Escherichia Coli.
Synonyms
Glucose-6-phosphate isomerase, Phosphoglucose isomerase, Phosphohexose isomerase, Autocrine motility factor, Neuroleukin, Sperm antigen 36, GPI, PGI, PHI, AMF, NLK, SA-36, GNPI.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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

GPI Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 578 amino acids (1-558 a.a.) and having a molecular mass of 65.3kDa.
The GPI is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glucose-6-phosphate isomerase (GPI) is an enzyme that plays a crucial role in energy metabolism. It belongs to the GPI family, whose members are involved in energy pathways. GPI exists as a dimer and catalyzes the interconversion of glucose-6-phosphate and fructose-6-phosphate. In mammals, GPI also acts as a cytokine secreted by tumors and an angiogenic factor (AMF) that promotes the movement of endothelial cells. Moreover, GPI functions as a neurotrophic factor called Neuroleukin, supporting the growth and survival of spinal and sensory neurons. GPI exhibits diverse roles both inside and outside the cell. Intracellularly, it participates in glycolysis and gluconeogenesis, while extracellularly, it acts as a neurotrophic factor for specific neuron types. Defects in the GPI gene can lead to nonspherocytic hemolytic anemia. Severe GPI deficiency is associated with hydrops fetalis, early neonatal death, and neurological impairment.
Description
This product consists of recombinant human GPI with a 20 amino acid His tag attached to its N-terminus. It is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 578 amino acids (residues 1-558). Its molecular weight is 65.3 kDa. The GPI protein undergoes purification using proprietary chromatographic methods.
Physical Appearance
Clear, colorless solution that is sterile-filtered.
Formulation
The GPI solution is provided at a concentration of 1 mg/ml in a buffer containing 20 mM Tris-HCl (pH 8.0), 1 mM DTT, and 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the product should be kept at 4°C. For long-term storage, it is recommended to freeze the product at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for extended storage. Repeated freezing and thawing should be avoided.
Purity
The purity of this product is greater than 95%, as assessed by SDS-PAGE analysis.
Synonyms
Glucose-6-phosphate isomerase, Phosphoglucose isomerase, Phosphohexose isomerase, Autocrine motility factor, Neuroleukin, Sperm antigen 36, GPI, PGI, PHI, AMF, NLK, SA-36, GNPI.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWYVSNIDGT HIAKTLAQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA STNGLINFIK QQREARVQ.

Product Science Overview

Biological Significance

GPI is ubiquitously present in most organisms, including humans. In mammals, this enzyme has multiple roles beyond its glycolytic function. It acts as an autocrine motility factor (AMF), a neuroleukin, and a maturation factor . These additional roles highlight its importance in various physiological processes, including cell motility, immune response, and neuronal development.

Genetic and Clinical Aspects

Deficiency in GPI activity is the second most common erythroenzymopathy of glycolytic enzymes, following pyruvate kinase deficiency . Inherited GPI deficiency can lead to hereditary nonspherocytic hemolytic anemia (HNSHA), a condition characterized by the destruction of red blood cells. Severe GPI deficiency can be associated with hydrops fetalis, immediate neonatal death, and neurological impairments .

Recombinant Production

Human recombinant GPI is typically expressed in Escherichia coli (E. coli) for research and therapeutic purposes . The recombinant enzyme is often tagged with a histidine tag at the C-terminal to facilitate purification. It is supplied as a solution in 50 mM Tris-HCl pH 7.5, and 50% glycerol .

Applications

Recombinant GPI is used in various biochemical and physiological studies. It is essential for understanding the enzyme’s role in glycolysis and its additional functions in different tissues. Moreover, it is used in the development of diagnostic tools and potential therapeutic agents for conditions related to GPI deficiency .

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