Recombinant Human PHGDH Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3807

Recombinant Human PHGDH Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-3807
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Product Overview

Tag His
Host Species Human
Accession O43175
Synonym 3-PGDH, 3PGDH, HEL-S-113, NLS, NLS1, PDG, PGAD, PGD, PGDH, PHGDHD, SERA
Background PHGDH is a member of the D-isomer specific 2-hydroxyacid dehydrogenase family. This new family consists of D-isomer-stereospecific enzymes. The conserved residues in this family appear to be the residues involved in the substrate binding and the catalytic reaction, and thus to be targets for site-directed mutagenesis. A number of NAD-dependent 2-hydroxyacid dehydrogenases which seem to be specific for the D-isomer of their substrate have been shown to be functionally and structurally related. PHGDH catalyzes the transition of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first and rate-limiting step in the phosphorylated pathway of serine biosynthesis, using NAD+/NADH as a cofactor. Overexpression of PHGDH may cause certain breast cancers. Defects in PHGDH are the cause of phosphoglycerate dehydrogenase deficiency which is characterized by congenital microcephaly, psychomotor retardation, and seizures.
Description A DNA sequence encoding the mature form of human PHGDH (O43175) (Met 1-Phe 533) was fused with a His tag at the C-terminus and an initial Met at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Met 1-Phe 533
Molecular Weight The recombinant human PHGDH comprises 543 a.a. and has a calculated molecular mass of 58KDa. It migrates as an approximately 55 kDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, 100mM Arg, 0.1% Tween20, 20% glycerol, pH 8.0.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate.
Protein Families D-isomer specific 2-hydroxyacid dehydrogenase family
Database References
Associated Diseases Phosphoglycerate dehydrogenase deficiency (PHGDHD); Neu-Laxova syndrome 1 (NLS1)

Gene Functions References

  1. PHGDH expression is regulated by PlncRNA-1 in breast cancer. PMID: 29626321
  2. Study provides evidence that a unique metabolic program is activated in a lung adenocarcinoma subset, described by PHGDH, which confers cell growth. PMID: 28614715
  3. Data indicate that the expression of PHGDH is increased in pancreatic cancer and is an independent molecular prognostic factor for pancreatic cancer patients. In addition, PHGDH controls cell proliferation, migration and invasion abilities. PMID: 29128633
  4. Data show there was a significant negative correlation between PHGDH copy-number alteration and EPAS1 (HIF2A) expression. PMID: 28951458
  5. Therefore, we show for the first time that the nuclear localization of Cat L and its substrate Cux1can be positively regulated by Snail NLS and importin beta1, suggesting that Snail, Cat L and Cux1 all utilize importin beta1 for nuclear import. PMID: 28698143
  6. High PHGDH expression is associated with idiopathic pulmonary fibrosis. PMID: 27836973
  7. This report present 6 individuals from 3 unrelated families with infantile serine biosynthesis defect due to PGDH deficiency. PMID: 28135894
  8. Overexpression of Phgdh may be generally associated with CK5 cells, and oncogenic function may be determined by isoform expression. PMID: 26026368
  9. High expression of PHGDH is associated with Colon Cancer. PMID: 26439504
  10. p53-mediated repression of PHGDH enhances the apoptotic response upon serine starvation in melanoma cells. PMID: 25404730
  11. Phosphoglycerate Dehydrogenase deficiency is associated with Neu-Laxova syndrome. PMID: 25152457
  12. We report on the identification of homozygous mutations in PHGDH and serine deficiency in individuals with Neu-Laxova syndrome. This disorder thus seems to be an extremely severe expression of PHGDH deficiency. PMID: 24836451
  13. PHGDH overexpression is found in cervical cancer, in particular, in bigger tumors and with advanced stages. Its expression is positively correlated with squamous cell carcinoma antigen level PMID: 24247658
  14. The potential mechanisms by which PHGDH promotes cancer are discussed. PMID: 21981974
  15. in some cancer cells a relatively large amount of glycolytic carbon is diverted into serine and glycine metabolism through phosphoglycerate dehydrogenase. PMID: 21804546
  16. results reveal that certain breast cancers are dependent upon increased serine pathway flux caused by PHGDH overexpression and demonstrate the utility of in vivo negative-selection RNAi screens for finding potential anticancer targets PMID: 21760589
  17. Studies in bacteria showed that addition of substrate at the active site is ordered, with HPAP binding before NADH. Also, NADH can compete with the substrate for binding to the allosteric site and thereby eliminate the substrate inhibition. PMID: 19388702
  18. The crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase has been solved with bound effector, 1-serine, and substrate, hydroxypyruvic acid phosphate. The human enzyme was also examined. PMID: 18627175
  19. The frequency of antibodies to Phgdh is much higher in patients with autoimmune hepatitis than in patients with other types of hepatitis or normal controls. PMID: 19497206
  20. PHGDH is expressed in cytoplasm of stromal and glandular cells in endometrium; expression is relatively high in proliferative phase and lower in secretory phase. Data suggest expression of PHGDH in endometrium is regulated by HOXA10. PMID: 19778996
  21. we conclude that this mutation impairs the folding and/or assembly of PHGDH but has minimal effects on the activity or stability of that portion of the V490M mutant that reaches a mature conformation PMID: 11751922
  22. These data suggest that missense mutations associated with 3-PGDH deficiency either primarily affect substrate binding or result in very low residual enzymatic activity. PMID: 19235232
  23. a coding PHGDH SNP (rs543703) was weakly associated with the development of schizophrenia in Korean population PMID: 19404161

FAQs

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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.

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