FBP1 Human, Active
Escherichia Coli.
Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.
Greater than 90.0% as determined by SDS-PAGE.
Description
FBP1 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-338) and having a molecular mass of 39.0 kDa.
FBP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
FBP1, or Fructose-1, 6-bisphosphatase 1, is an enzyme that plays a crucial role in glucose metabolism. It catalyzes the conversion of fructose 1, 6-bisphosphate to fructose 6-phosphate and inorganic phosphate. This reaction is a key step in gluconeogenesis, the process by which the body produces glucose from non-carbohydrate sources. Genetic mutations affecting the FBP1 enzyme can lead to metabolic disorders characterized by acidosis and low blood sugar.
This product consists of the FBP1 enzyme, recombinantly produced in E. coli bacteria. It is a single polypeptide chain that lacks glycosylation and contains 358 amino acids (specifically, amino acids 1 to 338), resulting in a molecular weight of 39.0 kDa. For purification and detection purposes, the FBP1 protein has a 20 amino acid His-Tag attached to its N-terminus. The purification process utilizes proprietary chromatographic methods.
The FBP1 protein solution is provided at a concentration of 1mg/ml. It is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 1mM DTT, and 10% glycerol.
The purity of the FBP1 protein is greater than 90.0%, as determined by SDS-PAGE analysis.
The specific activity of the FBP1 enzyme is measured to be greater than 7,000 pmol/min/ug. This is determined by monitoring the increase in absorbance at 340 nm, which corresponds to the reduction of NADP to NADPH during the enzymatic reaction. One unit of FBP1 activity is defined as the amount of enzyme that catalyzes the oxidation of 1.0 pmole of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate per minute at a pH of 9.5 and a temperature of 37°C.
Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.
Escherichia Coli.
MGSSHHHHHH SSGLVPRGSH MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ
Product Science Overview
Fructose-1,6-Bisphosphatase 1 (FBP1) is a crucial enzyme in the metabolic pathway of gluconeogenesis, which is the process of synthesizing glucose from non-carbohydrate sources. This enzyme catalyzes the hydrolysis of fructose-1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate, a key step in the regulation of glucose production in the liver . The human recombinant form of FBP1, often referred to as BioActive FBP1, is produced using recombinant DNA technology, ensuring high purity and activity for research and therapeutic applications.
FBP1 plays a pivotal role in maintaining blood glucose levels, especially during fasting or intense exercise when glucose reserves are low. It acts as a rate-limiting enzyme in gluconeogenesis, ensuring that glucose is produced efficiently to meet the body’s energy demands . Additionally, FBP1 is involved in regulating glucose sensing and insulin secretion in pancreatic beta-cells, and it modulates glycerol gluconeogenesis in the liver .
Deficiency in FBP1 activity can lead to metabolic disorders such as hypoglycemia and metabolic acidosis . Fructose-1,6-bisphosphatase deficiency is a rare genetic disorder characterized by an inability to properly regulate blood sugar levels, leading to episodes of low blood sugar and metabolic crises .
The human recombinant form of FBP1 is typically produced in bacterial or yeast expression systems. The gene encoding FBP1 is cloned into an expression vector, which is then introduced into the host cells. These cells are cultured under conditions that promote the expression of the FBP1 protein. The protein is then purified using techniques such as affinity chromatography, ensuring high purity and activity .
FBP1 catalyzes the conversion of fructose-1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations like magnesium (Mg2+) . This reaction is a critical control point in gluconeogenesis and is subject to complex allosteric regulation. The enzyme can exist in an active R-state or an inactive T-state, with intermediate conformations possible. Allosteric inhibitors such as AMP and fructose 2,6-bisphosphate play significant roles in regulating FBP1 activity .
