GPI Human, Active
Escherichia Coli.
Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.
Greater than 95.0% as determined by SDS-PAGE.
Description
GPIHuman Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 578 amino acids (1-558) and having a molecular mass of 65.3 kDa.
GPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Glucose-6-phosphate isomerase (GPI) is a crucial enzyme belonging to the phosphoglucose isomerase family, involved in energy metabolism pathways. This dimeric enzyme catalyzes the reversible conversion of glucose-6-phosphate to fructose-6-phosphate. In mammals, GPI exhibits additional roles as an angiogenic factor, tumor-secreted cytokine, and neurotrophic factor for spinal and sensory neurons.
Recombinant human GPI, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 65.3 kDa. The protein consists of 578 amino acids, encompassing residues 1-558, and incorporates a 20 amino acid His-Tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
The provided GPI solution has a concentration of 1 mg/ml and is formulated in a buffer containing 10% Glycerol, 1mM DTT, and 20mM Tris-HCl at a pH of 8.0.
The purity of the GPI protein is determined to be greater than 95% based on SDS-PAGE analysis.
The specific activity of GPI is measured to be greater than 400 units per mg of protein. This activity is determined by monitoring the increase in absorbance at 340 nm, reflecting the reduction of NADP to NADPH. One unit of GPI activity is defined as the amount of enzyme required to convert 1.0 micromole of D-Fructose 6-phosphate to D-glucose 6-phosphate per minute at a temperature of 37°C and pH of 7.4.
Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.
Escherichia Coli.
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
Glucose-6-Phosphate Isomerase (GPI), also known as phosphoglucose isomerase (PGI) or phosphohexose isomerase (PHI), is a crucial enzyme in the glycolytic pathway. It catalyzes the reversible isomerization of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P). This enzyme is ubiquitously present in most organisms and plays a significant role in energy metabolism.
GPI is a dimeric enzyme, meaning it consists of two identical subunits. In humans, the recombinant form of GPI is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain containing 578 amino acids with a molecular mass of approximately 65.3 kDa . The enzyme is purified using proprietary chromatographic techniques to ensure high purity and activity.
GPI performs multiple functions both inside and outside the cell:
- Intracellular Functions: Within the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, essential pathways for energy production and glucose metabolism.
- Extracellular Functions: Outside the cell, GPI acts as a neurotrophic factor (Neuroleukin) for spinal and sensory neurons, an angiogenic factor (Autocrine Motility Factor, AMF) that stimulates endothelial cell motility, and a tumor-secreted cytokine .
Defects in the GPI gene can lead to nonspherocytic hemolytic anemia, a condition characterized by the destruction of red blood cells. Severe enzyme deficiency can be associated with hydrops fetalis, immediate neonatal death, and neurological impairment . GPI deficiency is the second most common erythroenzymopathy of glycolytic enzymes after pyruvate kinase deficiency .
The human recombinant GPI is expressed in E. coli and is supplied as a sterile filtered, colorless solution. It is stable at 4°C for up to four weeks but should be stored desiccated below -18°C for long-term storage. To prevent freeze-thaw cycles, it is recommended to add a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) .
Recombinant GPI is used in various research and diagnostic applications, including studies on energy metabolism, cancer research, and neurobiology. Its multifunctional roles make it a valuable tool for understanding cellular processes and disease mechanisms.
