Recombinant Human Phosphoglycerate Kinase 1 (PGK1) Protein (GST)

Name: Recombinant Human Phosphoglycerate Kinase 1 (PGK1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03624P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Phosphoglycerate Kinase 1 (PGK1) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P00558
Target Symbol	PGK1
Synonyms	Cell migration-inducing gene 10 protein; Epididymis secretory sperm binding protein Li 68p; HEL S 68p; MGC117307; MGC8947; MIG10; pgk1; PGK1_HUMAN; PGKA; Phosphoglycerate kinase 1; Primer recognition protein 2; PRP 2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	FNVPMKNNQITNNQRIKAAVPSIKFCLDNGAKSVVLMSHLGRPDGVPMPDKYSLEPVAVELKSLLGKDVLFLKDCVGPEVEKACANPAAGSVILLENLRFHVEEEGKGKDASGNKVKAEPAKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPQKAGGFLMKKELNYFAKALESPERPFLAILGGAKVADKIQLINNMLDKVNEMIIGGGMAFTFLKVLNNMEIGTSLFDEEGAKIVKDLMSKAEKNGVKITLPVDFVTADKFDENAKTGQATVASGIPAGWMGLDCGPESSKKYAEAVTRAKQIVWNGPVGVFEWEAFARGTKALMDEVVKATSRGCITIIGGGDTATCCAKWNTEDKVSHVSTGGGASLELLEGKVLPGVDALSNI
Expression Range	25-417aa
Protein Length	Partial
Mol. Weight	68.9kDa
Research Area	Metabolism
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.