Recombinant Human PGK1 Protein (C-6His)

Name: Recombinant Human PGK1 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1595NP
Availability: InStock

BL-1595NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human Phosphoglycerate Kinase 1 is produced by our Mammalian expression system and the target gene encoding Ser2-Ile417 is expressed with a 6His tag at the C-terminus.
Accession	P00558
Synonym	Phosphoglycerate kinase 1;Cell migration-inducing gene 10 protein;Primer recognition protein 2;PGK1;PGKA
Gene Background	Phosphoglycerate kinase 1(PGK1) is an enzyme. It is mainly expressed in spermatogonia and Localized on the principle piece in the sperm. Its expression significantly decreased in the testis of elderly men. PGK1 involved in a critical energy-producing process known as glycolysis. It helps carry out a chemical reaction that converts a molecule called 1,3-diphosphoglycerate, which is produced during the breakdown of glucose, to another molecule called 3-phosphoglycerate during glycolysis. PGK1 may also act as a cofactor for polymerase alpha. The protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions.
Molecular Mass	45.5 KDa
Apmol Mass	37-50 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 20% Glycerol, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm motility.
Subcellular Location	Cytoplasm.
Protein Families	Phosphoglycerate kinase family
Database References	HGNC: 8896 OMIM: 300653 KEGG: hsa:5230 STRING: 9606.ENSP00000362413 UniGene: Hs.78771
Associated Diseases	Phosphoglycerate kinase 1 deficiency (PGK1D)
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.

Gene Functions References

PGK1 mutated variants display different catalytic activity and conformational stability compared to the native enzyme. PMID: 29995887
The results indicate that ALDOA and PGK1 may indicate resistance to cisplatin in osteosarcoma PMID: 29199648
PGK1 is used to indicate the prognosis of hepatocellular carcinoma (HCC). PMID: 28749413
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. PMID: 28923857
Acetylated PGK1 binds to and phosphorylates Beclin1 at S30, leading to activation of the VPS34-Beclin1 complex to initiate autophagosomal formation. PMID: 28238651
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) PMID: 28457968
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 PMID: 27342824
In neuroblastoma cells, CAIX and PGK1 expression is up regulated under hypoxia and correlates with response to targeted anti-proliferative treatment. PMID: 26510737
Mitochindrial PGK1 acts as a protein kinase in coordinating glycolysis and the tricarboxylic acid cycle, which is instrumental in cancer metabolism and tumorigenesis. PMID: 26942675
PI3K/AKT/mTOR pathway regulates HDAC3 S424 phosphorylation, which promotes HDAC3-PGK1 interaction and PGK1 K220 deacetylation PMID: 26356530
Retinal dystrophy may be one of the clinical manifestations of phosphoglycerate kinase deficiency. PMID: 26396085
mutations associated with hPGK1 deficiency lead to increased aggregation and proteolysis rates in vitro and inside cells due to protein thermodynamic destabilization PMID: 24838780
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. PMID: 25867275
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. PMID: 25175369
Phosphoglycerate kinase deficiency due to a novel mutation (c. 1180A>G) manifesting as chronic hemolytic anemia in a Japanese boy. PMID: 24934115
PGK1 appears to play an important role for neuroblastoma PMID: 24376734
different factors contributing to hPGK1 thermodynamic and kinetic stability PMID: 24721582
PGK1 could promote radioresistance in U251 human cells. PMID: 24284928
increased expression of PGK1 in colon cancer tissue is associated with metastasis. PMID: 23727790
Generif: Phosphoglycerate kinase is a moonlighting protein that functions as both a glycolytic enzyme and a primer recognition protein of DNA polymerase alpha. PMID: 2324090
Phosphoglycerate kinase is a moonlighting protein that functions as both a glycolytic enzyme and a disulfide reductase. PMID: 11130727
Conformational dynamics in the catalytic cycle of phosphoglycerate kinase, molecular details provided by structural analysis. [Review] PMID: 23684636
Glycolytic enzymes PGK1 and PKM2 are novel transcriptional targets of PPARgamma in breast cancer. PMID: 23130662
the low kinetic stability displayed by PGK1 protein mutations is causing human PGK1 deficiency PMID: 23336698
Phosphoglycerate kinase 1 was up-regulated significantly in radioresistant astrocytomas and also seems to be correlated with the negative prognosis following radiotherapy. PMID: 22742733
carbonic anhydrase I, phosphoglycerate kinase 1 and apolipoprotein A-I appeared to be the most significant variations of proteins in patients with osteopenia and osteoarthritis PMID: 22619369
two key (hub) PPARgamma direct target genes, PRKCZ and PGK1, were experimentally validated to be repressed upon PPARgamma activation by its natural ligand, 15d-PGJ2 in three prostrate cancer cell lines PMID: 21780947
All findings indicate that the different clinical manifestations associated with PGK1 deficiency chiefly depend on the distinctive type of perturbations caused by mutations in the PGK1 gene PMID: 22348148
enzyme kinetics studies show that the absence of the ribose OH-groups with is better tolerated for the purine than for the pyrimidine containing compounds in phosphoglycerate kinase 1 PMID: 21505655
Molecular dynamics simulations were carried out with four different nucleotides (D-/L-ADP and D-/L-CDP) in complex with PGK and 1,3-bisphospho-d-glycerate. The binding affinities of CDPs were very weak while D- and L-ADP were better substrates. PMID: 21549683
PGK domain movement and catalysis is regulated by a spring-loaded release mechanism PMID: 21349853
Phosphoglycerate kinase 1 (PGK1) showed a difference between follicular cells from follicles leading to a pregnancy or developmental failure. PMID: 19778949
PGK1-overexpressing fibroblasts with prostate tumor cells promoted tumor cell growth in vivo. Observations suggest that PGK1 helps support the interactions between cancer and its microenvironment. PMID: 20068185
Data show that PGK1 regulates the expression of CXCR4 and beta-catenin at the mRNA and protein levels. PMID: 19688824
Results suggest that conformational rearrangements in the hinge generated by binding of both substrates provide the main driving force for domain closure overcoming the slightly unfavourable contact interactions between the domains. PMID: 19854185
Phosphorylates pyrimidine L-deoxynucleoside analog diphosphaates PMID: 12080078
Overexpression induces a multidrug resistance phenotype. PMID: 12174867
3-phosphoglycerate kinase has a role in the activation of L-nucleoside analogs PMID: 12869554
These results demonstrate that phosphpglycerate kinase regulates uPAR expression at the post-transcriptional level. PMID: 14764427
production and secretion of PGK are regulated separately and oxygen and the protein hydroxylases can control not only gene expression but also protein secretion PMID: 15053920
phosphoglycerate kinase does not appear to have a role in the development or progression of neoplasms [letter] PMID: 15255553
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. PMID: 16363799
The impact of hypoxic treatment on the expression of PGK1 and the cytotoxicity of troxacitabine and gemcitabine are reported. PMID: 17565005
our study indicates that inhibition of the transcription mechanism is the cause of PGK deficiency. PMID: 17661373
Aa steady state kinetic and biophysical study of the interaction of the model compound l-MgADP with hPGK, is presented. PMID: 18096512
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. PMID: 18288812
overexpression of PGK1 and its signalling targets may be a expression-pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination PMID: 18453750
transmission path of the nucleotide effect toward the main hinge of phosphoglycerate kinase is described for the first time at the level of interactions existing in the tertiary structure[ 3-phosphoglycerate kinase] PMID: 18540639
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. PMID: 18603805

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