LDHA (Human) Recombinant Protein
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Specification
Product Description
Human LDHA (NP_005557, 1 a.a. - 332 a.a.) full-length recombinant protein with His tag expressed in Escherichia coli.
Sequence
MGSSHHHHHHSSGLVPRGSHMATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF
Host
Escherichia coli
Theoretical MW (kDa)
38.8
Form
Liquid
Preparation Method
Escherichia coli expression system
Purification
Conventional Chromatography
Concentration
0.5 mg/mL
Purity
> 95% by SDS-PAGE
Activity
Specific activity is > 20 units/mg. in which one unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37°C.
Quality Control Testing
Loading 3 ug protein in 15% SDS-PAGE
Storage Buffer
In 20 mM Tris-HCl buffer, 0.1 M NaCl, pH 8.0 (20% glycerol).
Storage Instruction
Store at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C.
Aliquot to avoid repeated freezing and thawing. -
Applications
Functional Study
SDS-PAGE
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Gene Info — LDHA
Entrez GeneID
3939Protein Accession#
NP_005557Gene Name
LDHA
Gene Alias
LDH-M, LDH1, PIG19
Gene Description
lactate dehydrogenase A
Omim ID
150000Gene Ontology
HyperlinkGene Summary
The protein encoded by this gene catalyzes the conversion of L-lactate and NAD to pyruvate and NADH in the final step of anaerobic glycolysis. The protein is found predominantly in muscle tissue and belongs to the lactate dehydrogenase family. Mutations in this gene have been linked to exertional myoglobinuria. Multiple transcript variants encoding different isoforms have been found for this gene. The human genome contains several non-transcribed pseudogenes of this gene. [provided by RefSeq
Other Designations
L-lactate dehydrogenase A|proliferation-inducing gene 19
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Interactome
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Pathway
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Disease
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Publication Reference
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Interrogating the lactate dehydrogenase tetramerization site using (stapled) peptides.
Léopold Thabault, Lucie Brisson, Chiara Brustenga, Santiago A Martinez Gache, Julien R C Prévost, Arina Kozlova, Quentin Spillier, Maxime Liberelle, Zohra Benyahia, Joris Messens, Tamara Copetti, Pierre Sonveaux, Raphaël Frédérick.
Journal of Medicinal Chemistry 2020 May; 63(9):4628.
Application：Enzyme, Func, Compound.
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Interrogating the lactate dehydrogenase tetramerization site using (stapled) peptides.
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