| Description | Acetate kinase belongs to acetate and sugar kinase/Hsc70/actin (ASKHA) structural superfamily.It exists as a dimer and has nucleotide binding site in the cleft between N and C-terminal domain.ApplicationAcetate Kinase from Escherichia coli has been used in assessing acetate kinase activity during Acetate kinase belongs to acetate and sugar kinase/Hsc70/actin (ASKHA) structural superfamily.It exists as a dimer and has nucleotide binding site in the cleft between N and C-terminal domain.ApplicationAcetate Kinase from Escherichia coli has been used in assessing acetate kinase activity during the fermatation process of Gluconacetobacter xylinus and in kinetic modeling and steady state studies.Acetate kinase is used to phosphorylate acetate to acetyl phosphate. Acetate Kinase from Escherichia coli has been used as part of an ATP-regenerating system to study the kinetics of agonist-stimulated transphosphatidylation.Physical formLyophilized powder containing trehalose with small amounts of potassium phosphate, magnesium chloride, and dithiothreitol... Read More | Inquire | Inquire | Store at -20°C. Store under desiccating conditions. The product can be stored for up to 12 months | Purity> 96% by SDS-PAGE and HPLC analyses.FunctionHas weak activities on human monocytes and acts via receptors that also recognize MIP-1 alpha. It induced intracellular Ca(2+) changes and enzyme release, but no chemotaxis, at concentrations of 100-1,000 nM, and was inactive on T-lymphocytes, Purity> 96% by SDS-PAGE and HPLC analyses.FunctionHas weak activities on human monocytes and acts via receptors that also recognize MIP-1 alpha. It induced intracellular Ca(2+) changes and enzyme release, but no chemotaxis, at concentrations of 100-1,000 nM, and was inactive on T-lymphocytes, neutrophils, and eosinophil leukocytes. Enhances the proliferation of CD34 myeloid progenitor cells. The processed form HCC-1(9-74) is a chemotactic factor that attracts monocytes eosinophils, and T-cells and is a ligand for CCR1, CCR3 and CCR5.Post-translationalThe N-terminal processed forms HCC-1(3-74), HCC-1(4-74) and HCC-1(9-74) are produced in small amounts by proteolytic cleavage after secretion in blood. HCC-1(1-74), but not HCC-1(3-74) and HCC-1(4-74), is partially O-glycosylated; the O-linked glycan consists of one Gal-GalNAc disaccharide, further modified by two N-acetylneuraminic acids... Read More |