Analytical Data
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Gene name
LDHA
- Application
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Alternative Names
LDHA;L-lactate dehydrogenase A chain
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P00338
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Expression Region
2-332aa
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AA Sequence
ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF
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Molecular Weight
44.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
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.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Lactate dehydrogenase A (LDHA) is a key enzyme in the glycolytic pathway, catalyzing the conversion of pyruvate to lactate while reducing NAD+ to NADH. Its pivotal role in metabolic processes has made LDHA a target of interest in various fields, including cancer research, metabolic disorders, and exercise physiology. In many tumors, LDHA is upregulated, promoting the Warburg effect, where cancer cells preferentially convert glucose to lactate even in the presence of oxygen, thereby supporting rapid cell proliferation. This has led researchers to investigate LDHA as a potential therapeutic target for cancer treatment. Moreover, its involvement in regulating lactate levels makes LDHA significant in conditions like ischemia and hypoxia, where metabolic adaptations are critical for cell survival. The production of recombinant LDHA proteins has enabled researchers to study its structure, function, and regulatory mechanisms in detail, leading to insights that could facilitate the development of LDHA inhibitors. The study of LDHA not only enhances our understanding of basic metabolic processes but also opens avenues for novel therapeutic strategies in managing diseases associated with metabolic dysregulation.
