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The protein encoded by PGK1 is a glycolytic enzyme that catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. Additionally we are shipping Phosphoglycerate Kinase 1 Antibodies (134) and Phosphoglycerate Kinase 1 Proteins (35) and many more products for this protein.
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In neuroblastoma (show ARHGEF16 ELISA Kits) cells, CAIX (show CA9 ELISA Kits) and PGK1 expression is up regulated under hypoxia and correlates with response to targeted anti-proliferative treatment.
Mitochindrial PGK1 acts as a protein kinase in coordinating glycolysis and the tricarboxylic acid cycle, which is instrumental in cancer metabolism and tumorigenesis.
PI3K (show PIK3CA ELISA Kits)/AKT (show AKT1 ELISA Kits)/mTOR (show FRAP1 ELISA Kits) pathway regulates HDAC3 (show HDAC3 ELISA Kits) S424 phosphorylation, which promotes HDAC3 (show HDAC3 ELISA Kits)-PGK1 interaction and PGK1 K220 deacetylation
Retinal dystrophy (show MERTK ELISA Kits) may be one of the clinical manifestations of phosphoglycerate kinase deficiency.
Results show that PGK1 mRNA and protein expression were significantly increased in breast cancer tissues and can be considered as a prognostic biomarker of chemoresistance to paclitaxel treatment in breast cancer.
Suppression of PGK1 enhanced the radiosensitivity of U251 xenografts and suggest that PGK1 may serve as a useful target in the treatment of radioresistant glioma.
Phosphoglycerate kinase deficiency due to a novel mutation (c. 1180A>G) manifesting as chronic hemolytic anemia in a Japanese boy.
PGK1 appears to play an important role for neuroblastoma (show ARHGEF16 ELISA Kits)
PGK1 could promote radioresistance in U251 human cells.
increased expression of PGK1 in colon cancer tissue is associated with metastasis.
present in, and accounts for, glycolysis and glutamate (show GRIN2A ELISA Kits) accumulation into synaptic vesicles
Phosphoglycerate kinase is a moonlighting protein that functions as both a glycolytic enzyme and a disulfide reductase (show GSR ELISA Kits).
Purification and characterization of 3-phosphoglycerate kinase from Ehrlich ascites carcinoma cells
PGK domain movement and catalysis is regulated by a spring-loaded release mechanism
Results indicate that COX-2 (show COX2 ELISA Kits) suppression by PGK-1 is independent of its catalytic activity.
Together, these data suggest that PGK1 secreted by PCa (show ENPP1 ELISA Kits) regulates bone formation at the metastatic site by increasing osteoblastic activity, decreasing osteoclastic function, and expressing an osteoblastic phenotype by PCa (show ENPP1 ELISA Kits) cells.
Heterozygous for the X-linked pgk-1a and pgk-1b. Clonally heterotypic glands with inactive X-specific methylation were present in the adult murine stomach.
Pgk1 is strongly expressed in the developing tooth germ of the mouse lower first molar.
Findings indicate that overexpression of PGK-1 in LLC-1 reduces the COX-2 (show COX2 ELISA Kits) expression, and, in turn, affect PGE2, cell invasion, angiogenesis, and the immune functions, and finally inhibit the tumor progression.
PGK1 (phosphoglycerate kinase 1) interacts with AtFtsZ2 in planta, suggesting a possible role in FtsZ phosphorylation.
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.
phosphoglycerate kinase 1
, PRP 2
, cell migration-inducing gene 10 protein
, primer recognition protein 2
, phosphoglycerate kinase