Name :
Recombinant Human 15-PGDH Protein (His Tag)
Biological Activity :
Background :
15-hydroxyprostaglandin dehydrogenase [NAD+], also known as Prostaglandin dehydrogenase 1, HPGD, and PGDH1, is a member of the short-chain dehydrogenases/reductases (SDR) family. Prostaglandins (PGs) play a key role in the onset of labor in many species and regulate uterine contractility and cervical dilatation. Therefore, the regulation of prostaglandin output by PG synthesizing and metabolizing enzymes in the human myometrium may determine uterine activity patterns in human labor both at preterm and at term. Prostaglandin dehydrogenase (PGDH) metabolizes prostaglandins (PGs) to render them inactive. HPGD is down-regulated by cortisol, dexamethasone, and betamethasone and down-regulated in colon cancer. It is up-regulated by TGFB1. HPGD contributes to the regulation of events that are under the control of prostaglandin levels. HPGD catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. and inhibits in vivo proliferation of colon cancer cells. Defects in HPGD are the cause of primary hypertrophic osteoarthropathy autosomal recessive (PHOAR), cranio-osteoarthropathy (COA), and isolated congenital nail clubbing.
Biological Activity :
Measured by the production of NADH during the oxidation of PGF2α. The specific activity is >1,500 pmoles/min/μg.
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
NP_000851.2
NCBI Gene ID :
Synonyms :
Synonyms :
hydroxyprostaglandin dehydrogenase 15-(NAD)
Amino Acid Sequence :
Molecular Weight :
The recombinant human HPGD comprises 272 amino acids and has a predicted molecular mass of 29.7 kDa. It migrates as an approximately 27 kDa band in SDS-PAGE under reducing conditions.
Purity :
> 92 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Endotoxin Level :
< 1.0 EU per μg protein as determined by the LAL method.
Protein Construction :
A DNA sequence encoding the human HPGD (NP_000851.2) (Met 1-Gln 266) was expressed, with a polyhistidine tag at the C-terminus.
Buffer Solution :
Supplied as sterile 50mM Tris, 100mM NaCl, 0.5mM DTT, 10% glycerol, pH 7.5Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
Liquid. It is shipped out with blue ice.
Redissolution :
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Synonyms :
15-PGDH Protein, Human; PGDH Protein, Human; PGDH1 Protein, Human; PHOAR1 Protein, Human; SDR36C1 Protein, Human 15-PGDH 背景信息 15-hydroxyprostaglandin dehydrogenase [NAD+], also known as Prostaglandin dehydrogenase 1, HPGD, and PGDH1, is a member of the short-chain dehydrogenases/reductases (SDR) family. Prostaglandins (PGs) play a key role in the onset of labor in many species and regulate uterine contractility and cervical dilatation. Therefore, the regulation of prostaglandin output by PG synthesizing and metabolizing enzymes in the human myometrium may determine uterine activity patterns in human labor both at preterm and at term. Prostaglandin dehydrogenase (PGDH) metabolizes prostaglandins (PGs) to render them inactive. HPGD is down-regulated by cortisol, dexamethasone, and betamethasone and down-regulated in colon cancer. It is up-regulated by TGFB1. HPGD contributes to the regulation of events that are under the control of prostaglandin levels. HPGD catalyzes the NAD-dependent dehydrogenation of lipoxin A4 to form 15-oxo-lipoxin A4. and inhibits in vivo proliferation of colon cancer cells. Defects in HPGD are the cause of primary hypertrophic osteoarthropathy autosomal recessive (PHOAR), cranio-osteoarthropathy (COA), and isolated congenital nail clubbing.
References & Citations :
Patel, FA. et al., 2003, J. Clin. Endocrinol. Metab. 88: 2922-33. McKeown KJ, et al.,2003, J. Clin. Endocrinol. Metab. 88 (4): 1737-41. Yan, M. et al., 2004, Proc. Natl. Acad. Sci. USA. 101: 17468-73. Tariq, M. et al., 2009, J Med Genet. 46 (1): 14-20.
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