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Human Polyclonal PGK1 Primary Antibody pour FACS, IF - ABIN391135
Danshina, Geyer, Dai, Goulding, Willis, Kitto, McCarrey, Eddy, OBrien: Phosphoglycerate kinase 2 (PGK2) is essential for sperm function and male fertility in mice. dans Biology of reproduction 2009
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Human Polyclonal PGK1 Primary Antibody pour IHC (p), ELISA - ABIN542998
Shetty, Muniyappa, Halady, Idell: Regulation of urokinase receptor expression by phosphoglycerate kinase. dans American journal of respiratory cell and molecular biology 2004
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Human Polyclonal PGK1 Primary Antibody pour ELISA, WB - ABIN543580
West, Moore, Biskup, Bugayenko, Smith, Ross, Dawson, Dawson: Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. dans Proceedings of the National Academy of Sciences of the United States of America 2005
Human Polyclonal PGK1 Primary Antibody pour IHC (p), WB - ABIN391250
Garzón, Gayarre, Gharbi, Díez-Dacal, Sánchez-Gómez, Timms, Pérez-Sala: A biotinylated analog of the anti-proliferative prostaglandin A1 allows assessment of PPAR-independent effects and identification of novel cellular targets for covalent modification. dans Chemico-biological interactions 2009
Human Polyclonal PGK1 Primary Antibody pour ELISA, ICC - ABIN4345073
Khurana, Laskar, Bhattacharyya, Bhattacharyya: Hsp90 induces increased genomic instability toward DNA-damaging agents by tuning down RAD53 transcription. dans Molecular biology of the cell 2016
High PGK1 expression was associated with poor prognosis in breast cancer, because PGK1 and HIF-1alpha formed a positive feed-forward loop and thus stimulated breast cancer progression and metastases.
PGK1 mutated variants display different catalytic activity and conformational stability compared to the native enzyme.
The results indicate that ALDOA and PGK1 may indicate resistance to cisplatin in osteosarcoma
PGK1 is used to indicate the prognosis of hepatocellular carcinoma (HCC).
Data show that LINC00963 (MetaLnc9) interacted with the glycolytic kinase PGK1 and prevented its ubiquitination in non-small cell lung cancer (NSCLC) cells, leading to activation of the oncogenic AKT/mTOR signaling pathway.
Acetylated PGK1 binds to and phosphorylates Beclin1 at S30, leading to activation of the VPS34-Beclin1 complex to initiate autophagosomal formation.
Data suggest that, in breast cancer cells, MYC acts as an upstream regulator leading to PGK1 activation. (MYC, proto-oncogene c-myc; PGK1, phosphoglycerate kinase 1)
PGK1, a glycolytic enzyme catalyzing the conversion of 3-phosphoglycerate into 2-phosphoglycerate, has increased expression in synovial tissues and blood of rheumatoid arthritis, which may be involved in pro-inflammation and synovial hyperplasia of the disease
In neuroblastoma cells, CAIX 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/AKT/mTOR pathway regulates HDAC3 S424 phosphorylation, which promotes HDAC3-PGK1 interaction and PGK1 K220 deacetylation
Retinal dystrophy may be one of the clinical manifestations of phosphoglycerate kinase deficiency.
mutations associated with hPGK1 deficiency lead to increased aggregation and proteolysis rates in vitro and inside cells due to protein thermodynamic destabilization
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
different factors contributing to hPGK1 thermodynamic and kinetic stability
PGK1 could promote radioresistance in U251 human cells.
increased expression of PGK1 in colon cancer tissue is associated with metastasis.
Pgk1 overexpression, or treatment with terazosin (an FDA-approved small molecule that binds and activates Pgk1), rescued motor axon phenotypes in SMA zebrafish. We conclude that global bioenergetics pathways can be therapeutically manipulated to ameliorate SMA motor neuron phenotypes in vivo.
Phosphoglycerate kinase is a moonlighting protein that functions as both a glycolytic enzyme and a disulfide reductase.
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 suppression by PGK-1 is independent of its catalytic activity.
Together, these data suggest that PGK1 secreted by PCa regulates bone formation at the metastatic site by increasing osteoblastic activity, decreasing osteoclastic function, and expressing an osteoblastic phenotype by PCa 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 expression, and, in turn, affect PGE2, cell invasion, angiogenesis, and the immune functions, and finally inhibit the tumor progression.
targeting of a single bioenergetic protein, phosphoglycerate kinase 1 (Pgk1), was found to modulate motor neuron vulnerability in vivo. Knockdown of pgk1 alone was sufficient to partially mimic the SMA phenotype in wild-type zebrafish
present in, and accounts for, glycolysis and glutamate accumulation into synaptic vesicles
PGK1 role in metabolism and growth.
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.
, cell migration-inducing gene 10 protein
, primer recognition protein 2
, phosphoglycerate kinase
, phosphoglycerate kinase 1
, phosphoglycerate kinase 2