Anti Glyoxylate And Hydroxypyruvate Reductase (GRHPR) C-terminal region mAb (Clone 7G1)

Cosmo Bio LTD

Catalog No: KAL-KC595

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Application: ELISA, WB 
Clonality: Monoclonal 
Host: Mouse 
Purification: Ig-PG 
Reactivity: Human 
UniPlot Summary
//Function Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduceshydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
//Catalytic activity Glycolate + NADP+ = glyoxylate + NADPH. D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H.//Subunit structure Homodimer. Ref.1 Ref.7
//Tissue specificity Ubiquitous. Most abundantly expressed in the liver. Ref.5
//Involvement in disease Defects in GRHPR are the cause of hyperoxaluria primary type 2 (HP2) [MIM:260000]; also known as primaryhyperoxaluriatype II (PH2). HP2 is a disorder where the main clinical manifestation is calcium oxalatenephrolithiasis though chronic as wellas terminal renal insufficiency has been described. It is characterized by an elevated urinary excretion of oxalate and L-glycerate. Ref.2
//Sequence similarities Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Reference
1. "Identification and expression of a cDNA for human hydroxypyruvate/glyoxylatereductase." Rumsby G. et al. Biochim. Biophys. Acta1446:383-388(1999) [PubMed: 10524214] [Abstract]. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT. Tissue: Liver.
2. "The gene encoding hydroxypyruvatereductase (GRHPR) is mutated in patients with primary hyperoxaluria type II." Cramer S.D. et al.Hum. Mol. Genet. 8:2063-2069(1999) [PubMed: 10484776] [Abstract]. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA],INVOLVEMENT IN HP2. Tissue: Liver.
3. Liu B. et al. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALEMRNA]. Tissue: Aorta