|Application ||IHC-P, FC, IF, WB|
|Other Accession||P16617, P09411, Q60HD8|
|Predicted||Mouse, Rat, Monkey|
|Calculated MW||H=45;M=45;Rat=45 KDa|
|Other Names||PGK1; PGKA; Phosphoglycerate kinase 1; Cell migration-inducing gene 10 protein; Primer recognition protein 2|
|Target/Specificity||This PGK1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 117-145 amino acids from the Central region of human PGK1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PGK1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein) (PubMed:2324090). May play a role in sperm motility (PubMed:26677959).|
|Tissue Location||Mainly expressed in spermatogonia. Localized on the principle piece in the sperm (at protein level). Expression significantly decreased in the testis of elderly men|
Provided below are standard protocols that you may find useful for product applications.
Also known as ATP:3-phosphoglycerate 1-phosphotransferase (EC 220.127.116.11), this major enzyme in glycolysis catalyzes the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate, generating one molecule of ATP. New blood vessel formation or angiogenesis is critical for tumor expansion and metastasis. Lay et al. (2000) showed that the plasmin reductase isolated from conditioned medium of fibrosarcoma cells is the glycolytic enzyme phosphoglycerate kinase. They concluded that phosphoglycerate kinase not only functions in glycolysis but is secreted by tumor cells and participates in the angiogenic process as a disulfide reductase.
Lay, A. J., et al. Nature 408: 869-873 (2000).