Full Product Name
PKLR Antibody
Product Gene Name
anti-PKLR antibody
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Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
3D Structure
ModBase 3D Structure for P30613
Other Notes
Small volumes of anti-PKLR antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
NCBI/Uniprot data below describe general gene information for PKLR. It may not necessarily be applicable to this product.
NCBI Accession #
NP_000289.1
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NCBI GenBank Nucleotide #
NM_000298.6
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UniProt Primary Accession #
P30613
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UniProt Secondary Accession #
O75758; P11973[Other Products]
UniProt Related Accession #
P30613[Other Products]
Molecular Weight
58,494 Da
NCBI Official Full Name
pyruvate kinase PKLR isoform 1
NCBI Official Synonym Full Names
pyruvate kinase L/R
NCBI Official Symbol
PKLR [Similar Products]
NCBI Official Synonym Symbols
PK1; PKL; PKR; RPK; PKRL
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NCBI Protein Information
pyruvate kinase PKLR
UniProt Protein Name
Pyruvate kinase PKLR
UniProt Synonym Protein Names
Pyruvate kinase 1; Pyruvate kinase isozymes L/R; R-type/L-type pyruvate kinase; Red cell/liver pyruvate kinase
Protein Family
Pyruvate kinase
UniProt Gene Name
PKLR [Similar Products]
UniProt Synonym Gene Names
PK1; PKL [Similar Products]
NCBI Summary for PKLR
The protein encoded by this gene is a pyruvate kinase that catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP, which is the rate-limiting step of glycolysis. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
UniProt Comments for PKLR
Plays a key role in glycolysis.
Research Articles on PKLR
1. Results show that different residues contribute to the two allosteric functions: regulation by the activator fructose-1,6-bisphosphate (Fru-1,6-BP) and alanine, the inhibitor. Only a small fraction of mutated residues perturbed inhibition by alanine. In contrast, a large percentage of mutated residues influenced activation by Fru-1,6-BP; inhibition by alanine is not simply the reverse of activation by Fru-1,6-BP.
Precautions
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Disclaimer
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