PGK1 Antibody, HRP conjugated

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Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
We typically dispatch products within 1-3 business days after receiving your order. Delivery times may vary depending on the shipping method and destination. Please consult your local distributor for specific delivery timeframes.
Synonyms
Cell migration-inducing gene 10 protein antibody; Epididymis secretory sperm binding protein Li 68p antibody; HEL S 68p antibody; MGC117307 antibody; MGC8947 antibody; MIG10 antibody; pgk1 antibody; PGK1_HUMAN antibody; PGKA antibody; Phosphoglycerate kinase 1 antibody; Primer recognition protein 2 antibody; PRP 2 antibody
Target Names
Uniprot No.

Target Background

Function
PGK1 catalyzes one of the two ATP-producing reactions in the glycolytic pathway, facilitating the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. Beyond its role in glycolysis, PGK1 appears to function as a polymerase alpha cofactor protein (primer recognition protein). It may also contribute to sperm motility.
Gene References Into Functions
  1. Mutated variants of PGK1 exhibit altered catalytic activity and conformational stability compared to the native enzyme. PMID: 29995887
  2. Research suggests that ALDOA and PGK1 may be associated with resistance to cisplatin in osteosarcoma. PMID: 29199648
  3. PGK1 expression levels are considered a potential prognostic indicator for hepatocellular carcinoma (HCC). PMID: 28749413
  4. Studies indicate that LINC00963 (MetaLnc9) interacts with PGK1, preventing its ubiquitination in non-small cell lung cancer (NSCLC) cells. This interaction leads to the activation of the oncogenic AKT/mTOR signaling pathway. PMID: 28923857
  5. Acetylated PGK1 binds to and phosphorylates Beclin1 at S30, activating the VPS34-Beclin1 complex to initiate autophagosomal formation. PMID: 28238651
  6. Research suggests that MYC acts as an upstream regulator, leading to PGK1 activation in breast cancer cells. (MYC, proto-oncogene c-myc; PGK1, phosphoglycerate kinase 1) PMID: 28457968
  7. PGK1, a glycolytic enzyme responsible for the conversion of 3-phosphoglycerate into 2-phosphoglycerate, exhibits increased expression in synovial tissues and blood of rheumatoid arthritis patients. This suggests a potential involvement in pro-inflammation and synovial hyperplasia associated with the disease. PMID: 27342824
  8. In neuroblastoma cells, the expression of CAIX and PGK1 is upregulated under hypoxic conditions and correlates with the response to targeted anti-proliferative treatment. PMID: 26510737
  9. Mitochondrial PGK1 functions as a protein kinase, coordinating glycolysis and the tricarboxylic acid cycle. This coordination is crucial for cancer metabolism and tumorigenesis. PMID: 26942675
  10. The PI3K/AKT/mTOR pathway regulates HDAC3 S424 phosphorylation, promoting HDAC3-PGK1 interaction and PGK1 K220 deacetylation. PMID: 26356530
  11. Retinal dystrophy may be a clinical manifestation of phosphoglycerate kinase deficiency. PMID: 26396085
  12. Mutations associated with hPGK1 deficiency lead to increased aggregation and proteolysis rates in vitro and in cells due to protein thermodynamic destabilization. PMID: 24838780
  13. Research indicates that PGK1 mRNA and protein expression are significantly elevated in breast cancer tissues. It may serve as a prognostic biomarker for chemoresistance to paclitaxel treatment in breast cancer. PMID: 25867275
  14. Suppression of PGK1 enhances the radiosensitivity of U251 xenografts, suggesting that PGK1 might be a potential therapeutic target for radioresistant glioma. PMID: 25175369
  15. Phosphoglycerate kinase deficiency due to a novel mutation (c. 1180A>G) has been observed as chronic hemolytic anemia in a Japanese boy. PMID: 24934115
  16. PGK1 appears to play a significant role in neuroblastoma. PMID: 24376734
  17. Various factors contribute to the thermodynamic and kinetic stability of hPGK1. PMID: 24721582
  18. PGK1 may promote radioresistance in U251 human cells. PMID: 24284928
  19. Increased PGK1 expression in colon cancer tissue is associated with metastasis. PMID: 23727790
  20. Phosphoglycerate kinase is a moonlighting protein exhibiting dual functionality as both a glycolytic enzyme and a primer recognition protein for DNA polymerase alpha. PMID: 2324090
  21. Phosphoglycerate kinase also demonstrates moonlighting activity as a disulfide reductase. PMID: 11130727
  22. Structural analysis provides molecular details regarding conformational dynamics in the catalytic cycle of phosphoglycerate kinase. [Review] PMID: 23684636
  23. Glycolytic enzymes PGK1 and PKM2 are novel transcriptional targets of PPARgamma in breast cancer. PMID: 23130662
  24. The low kinetic stability exhibited by PGK1 protein mutations is a contributing factor to human PGK1 deficiency. PMID: 23336698
  25. Phosphoglycerate kinase 1 is significantly upregulated in radioresistant astrocytomas and is also associated with a poor prognosis after radiotherapy. PMID: 22742733
  26. Carbonic anhydrase I, phosphoglycerate kinase 1, and apolipoprotein A-I appear to be the most significantly altered proteins in patients with osteopenia and osteoarthritis. PMID: 22619369
  27. 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 prostate cancer cell lines. PMID: 21780947
  28. Findings indicate that the diverse clinical manifestations associated with PGK1 deficiency primarily depend on the specific type of disruptions caused by mutations in the PGK1 gene. PMID: 22348148
  29. Enzyme kinetics studies demonstrate that the absence of the ribose OH-groups is better tolerated for purine-containing compounds than for pyrimidine-containing compounds in phosphoglycerate kinase 1. PMID: 21505655
  30. Molecular dynamics simulations were conducted 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 proved to be better substrates. PMID: 21549683
  31. PGK domain movement and catalysis are regulated by a spring-loaded release mechanism. PMID: 21349853
  32. Phosphoglycerate kinase 1 (PGK1) exhibited differences between follicular cells from follicles leading to pregnancy and those leading to developmental failure. PMID: 19778949
  33. Fibroblasts overexpressing PGK1 in the presence of prostate tumor cells promoted tumor cell growth in vivo. Observations suggest that PGK1 supports interactions between cancer and its microenvironment. PMID: 20068185
  34. Data indicate that PGK1 regulates the expression of CXCR4 and beta-catenin at the mRNA and protein levels. PMID: 19688824
  35. Results suggest that conformational rearrangements in the hinge, generated by binding of both substrates, provide the main driving force for domain closure. This overcomes slightly unfavorable contact interactions between the domains. PMID: 19854185
  36. PGK1 phosphorylates pyrimidine L-deoxynucleoside analog diphosphates. PMID: 12080078
  37. Overexpression of PGK1 induces a multidrug resistance phenotype. PMID: 12174867
  38. 3-phosphoglycerate kinase plays a role in the activation of L-nucleoside analogs. PMID: 12869554
  39. Research demonstrates that phosphoglycerate kinase regulates uPAR expression at the post-transcriptional level. PMID: 14764427
  40. Production and secretion of PGK are regulated independently, and oxygen and protein hydroxylases can control both gene expression and protein secretion. PMID: 15053920
  41. Phosphoglycerate kinase does not appear to have a role in the development or progression of neoplasms. [letter] PMID: 15255553
  42. During domain closure, Lys 215 in 3-phosphoglycerate kinase likely moves along with the transferring phosphate, ensuring proper positioning for catalysis. PMID: 16363799
  43. The impact of hypoxic treatment on the expression of PGK1 and the cytotoxicity of troxacitabine and gemcitabine has been studied. PMID: 17565005
  44. Research suggests that inhibition of the transcription mechanism is the cause of PGK deficiency. PMID: 17661373
  45. A steady-state kinetic and biophysical study of the interaction between the model compound l-MgADP and hPGK is presented. PMID: 18096512
  46. While L-ADP is almost as catalytically competent as D-ADP, under specific experimental conditions (buffer containing 30% methanol, 4 degrees C), phosphoglycerate kinase binds D- and L-ADP with similar kinetics. PMID: 18288812
  47. Overexpression of PGK1 and its signaling targets might be a contributing pathway in diffuse primary gastric carcinomas promoting peritoneal dissemination. PMID: 18453750
  48. The transmission path of the nucleotide effect towards 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
  49. PGK1 was selectively overexpressed in human colon tumor cells after treatment with hydrogen peroxide as oxidative stress. Its expression was suppressed by co-treatment with antioxidants. PMID: 18603805

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Database Links

HGNC: 8896

OMIM: 300653

KEGG: hsa:5230

STRING: 9606.ENSP00000362413

UniGene: Hs.78771

Involvement In Disease
Phosphoglycerate kinase 1 deficiency (PGK1D)
Protein Families
Phosphoglycerate kinase family
Subcellular Location
Cytoplasm.
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.

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