protein

Enolase 1/ENO1 Protein, Human (C-His)

HY-P70260A

5 μg;10 μg;50 μg;100 μg

90;150;420;710 USD

Enolase 1/ENO1 Protein, Human (C-His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

90;150;420;710 USD

The ENO1 protein converts 2-phosphoglycerate to phosphoenolpyruvate and is involved in growth control, hypoxia tolerance, and allergic responses. It acts as a receptor and activator of plasminogen, stimulating immunoglobulin production. ENO1 binds to the myc promoter as a transcriptional repressor and may function as a tumor suppressor. Enolase 1/ENO1 Protein, Human (C-His) is the recombinant human-derived Enolase 1/ENO1 protein, expressed by E. coli , with C-6*His labeled tag.

Human

The ENO1 Protein operates as a glycolytic enzyme, catalyzing the conversion of 2-phosphoglycerate to phosphoenolpyruvate. In addition to its role in glycolysis, ENO1 is implicated in various processes such as growth control, hypoxia tolerance, and allergic responses. Notably, it displays versatility by potentially functioning in the intravascular and pericellular fibrinolytic system, acting as a receptor and activator of plasminogen on the cell surface of diverse cell types including leukocytes and neurons. ENO1's ability to stimulate immunoglobulin production further underscores its multifaceted functions. Moreover, it binds to the myc promoter and acts as a transcriptional repressor, suggesting a regulatory role in gene expression. Additionally, ENO1 may function as a tumor suppressor, implicating its involvement in cellular processes that extend beyond glycolysis and impact critical aspects of growth control and immune responses.

rHuAlpha-enolase, His; Alpha-enolase; 2-phospho-D-glycerate hydro-lyase; C-myc promoter-binding protein; Enolase 1; MBP-1; MPB-1; Non-neural enolase; NNE; Phosphopyruvate hydratase; Plasminogen-binding protein; ENO1

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

Lyophilized from a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 8.0.

Room temperature in continental US; may vary elsewhere.