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Validated All-in-One™ qPCR Primer for PGK1(NM_000291.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
The protein encoded by this gene is a glycolytic enzyme that catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. The encoded protein may also act as a cofactor for polymerase alpha. This gene lies on the X-chromosome, while a related pseudogene also has been found on the X-chromosome and another on chromosome 19. [provided by RefSeq].
Gene References into function
- Phosphorylates pyrimidine L-deoxynucleoside analog diphosphaates
- Overexpression induces a multidrug resistance phenotype.
- 3-phosphoglycerate kinase has a role in the activation of L-nucleoside analogs
- These results demonstrate that phosphpglycerate kinase regulates uPAR expression at the post-transcriptional level.
- production and secretion of PGK are regulated separately and oxygen and the protein hydroxylases can control not only gene expression but also protein secretion
- phosphoglycerate kinase does not appear to have a role in the development or progression of neoplasms [letter]
- During domain closure, Lys 215 in 3-phosphoglycerate kinase possibly moves together with the transferring phosphate, and this group is being positioned properly for catalysis.
- The impact of hypoxic treatment on the expression of PGK1 and the cytotoxicity of troxacitabine and gemcitabine are reported.
- our study indicates that inhibition of the transcription mechanism is the cause of PGK deficiency.
- Aa steady state kinetic and biophysical study of the interaction of the model compound l-MgADP with hPGK, is presented.
- Although L-ADP is almost as catalytically competent as D-ADP, under our experimental conditions (buffer containing 30% methanol, 4 degrees C) phosphoglycerate kinase binds D- and L-ADP with similar kinetics.
- overexpression of PGK1 and its signalling targets may be a expression-pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination
- PGK1 was selectively overexpressed in human colon tumor cells by treating with hydrogen peroxide as oxidative stress, while its expression was suppressed by co-treatment with antioxidants.
- This protein has been found differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
