protein

Glucose-6-phosphate isomerase Protein, Human (His)

HY-P71680

5 μg;10 μg;50 μg

119;203;568 USD

Glucose-6-phosphate isomerase Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg

119;203;568 USD

Glucose-6-phosphate isomerase protein is a key player in glycolysis, catalyzing the conversion of glucose-6-phosphate into fructose-6-phosphate in the cytoplasm. It carries out this reaction reversibly during gluconeogenesis. Glucose-6-phosphate isomerase Protein, Human (His) is the recombinant human-derived Glucose-6-phosphate isomerase protein, expressed by E. coli , with N-6*His labeled tag.

Human

In the cytoplasm, the Glucose-6-phosphate isomerase protein plays a pivotal role in glycolysis by catalyzing the conversion of glucose-6-phosphate to fructose-6-phosphate, representing the second step in this metabolic pathway, and it reversibly performs this reaction during gluconeogenesis. Beyond its function as a glycolytic enzyme, this protein exhibits additional roles as a secreted cytokine. Functioning as an angiogenic factor (AMF), it stimulates endothelial cell motility, contributing to angiogenesis. Moreover, Glucose-6-phosphate isomerase acts as a neurotrophic factor, known as neuroleukin, specifically benefiting spinal and sensory neurons. Notably, it is secreted by lectin-stimulated T-cells, where it induces immunoglobulin secretion, highlighting its diverse and multifunctional roles both intracellularly and extracellularly in various physiological processes.

AMF; Aurocrine motility factor; Autocrine motility factor; DKFZp686C13233; EC 5.3.1.9; Neuroleukin; NLK; Oxoisomerase; PGI; PHI; Phosphoglucose isomerase; SA-36; SA36; Sperm antigen 36

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm sterile filtered PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US; may vary elsewhere.