34 products were found matching "P4076-73"!

Phosphorylation and dephosphorylation of cellular proteins are central steps in transducing extracellular signals to the cell nucleus. Phosphorylated epitopes may serve as docking sites for the assembly of protein complexes or may alter the 3-dimensional protein structure thus modulating enzymatic activity or the...

Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Applications: Suitable for use in ELISA and Western Blot. Other applications not tested. Recommended Dilution: ELISA: 1:32,000, Western Blot: 0.05-1ug/ml,...

Changes in the serine/threonine phosphorylation state of a protein in response to various external stimuli can have profound effects on cellular signal transduction, apoptosis and carcinogenesis. The reagents, including phosphorylated proteins, peptides, and antibodies against the phosphospecific amino acid, are...

Phosphorylation and dephosphorylation of cellular proteins are central steps in transducing , extracellular signals to the cell nucleus. Phosphorylated epitopes may serve as docking sites for , the assembly of protein complexes or may alter the 3-dimensional protein structure thus , modulating enzymatic activity or...

Phosphorylation and dephosphorylation of cellular proteins are central steps in transducing extracellular signals to the cell nucleus. Phosphorylated epitopes may serve as docking sites for the assembly of protein complexes or may alter the 3-dimensional protein structure thus modulating enzymatic activity or the...

Human phosphoserine phosphatase (HPSP), specific for D- and L- phosphoserine, has been , identified in all human tissues. HPSP is a Mg(2+)-dependent phosphoserine phosphatase. The three dimensional structure of HPSP reveals the structural and functional role of the divalent cation in the active site of phosphatases....

Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction...

Protein phosphorylation is an important post-translational modification that serves many key functions to regulate a protein's activity, localization, and protein-protein interactions. Phosphorylation is catalyzed by various specific protein kinases, which involves removing a phosphate group from ATP and covalently...

Protein phosphorylation is an important post-translational modification that serves many key functions to regulate a protein's activity, localization, and protein-protein interactions. Phosphorylation is catalyzed by various specific protein kinases, which involves removing a phosphate group from ATP and covalently...

Phosphorylation and dephosphorylation of cellular proteins are central steps in transducing extracellular signals to the cell nucleus. Phosphorylated epitopes may serve as docking sites for the assembly of protein complexes or may alter the 3-dimensional protein structure thus modulating enzymatic activity or the...

Phosphoinositide 3 Kinase, Recombinant, Bovine, p85 alpha (PI3K) functions as the regulatory subunit of the class IA PI3-kinase isoforms a, b, and d. It contains two SH2 domains that bind to tyrosine-phosphorylated growth factor receptors or substrate adaptor proteins. It also contains a BH (breakpoint cluster...

PGD (Phosphogluconate dehydrogenas), also known as 6PGD, is a 483 amino acid enzyme that is involved in the pentose phosphate shunt. Pentose is required for nucleic acid biosynthesis and the pentose phosphate cycle is a major source of NADPH. PGD deficiency increases the level of erythrocyte pyruvate kinase (PK)...