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Phosphopyruvate hydratase

" in MedChemExpress (MCE) Product Catalog:
Cat. No. Compare Product Name Species Source
  • HY-P70260A

    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

    Human E. coli
    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. 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. The total length of Enolase 1/ENO1 Protein, Human (C-His) is 434 a.a., with molecular weight of 49 kDa.
  • HY-P70260

    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

    Human E. coli
    Alpha-enolase/Enolase 1 Protein, Human (His) expresses in E. coli with a His tag at the N-terminus. Alpha-enolase, a multifunctional protein, is a key glycolytic enzyme in the cytoplasm of prokaryotic and eukaryotic cells.

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