PGK1 Recombinant Rabbit Monoclonal Antibody [ST49-07]

Function

Phosphoglycerate kinases 1/2 (PGK1/2, ATP:3-phospho-D-glycerate 1-phosphotransferase, EC 2.7.2.3) are somatically expressed, glycolytic enzymes that catalyze the transfer of a phosphoryl group from the acyl phosphate of 1,3-bisphosphoglycerate to ADP, thereby forming ATP and 3-phosphoglycerate. The human PGK gene is interrupted by 10 introns and spans 23 kilobases, and is X chromosome-linked at position Xq21.1, a region implicated in prostate cancer, androgen insensitivity, perineal hypospadias, and other genetic abnormalities. In addition to influencing glycolysis, the PGK1 is secreted by tumor cells and contributes to proliferative angiogenic processes as a disulfide reductase. PGK1 mediated reduction of disulphide bonds in the serine proteinase plasmin initiates the release of the tumor blood vessel inhibitor angiostatin, an event that is critical for blood vessel formation or angiogenesis in tumor expansion and metastasis.

Background References

1. Trahey, M. et al. 2012. Poliovirus infection transiently increases COPII vesicle budding. J. Virol. 86: 9675-82.

2. Marzano, V. et al. 2012. Proteomic profiling of ATM kinase proficient and deficient cell lines upon blockage of proteasome activity. J Proteomics. 75: 4632-4646.

Sequence Similarity

Belongs to the phosphoglycerate kinase family.

Tissue Specificity

Mainly expressed in spermatogonia. Localized on the principle piece in the sperm (at protein level). Expression significantly decreased in the testis of elderly men.

Subcellular Location

Cytoplasm.

UNIPROT

SwissProt: P00558 Human

SwissProt: P09411 Mouse

SwissProt: P16617 Rat

Synonyms