Analytical Data
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Gene name
LDHB
- Application
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Alternative Names
LDHB；L-lactate dehydrogenase B 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
P07195
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Expression Region
2-334aa
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AA Sequence
ATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL
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Molecular Weight
43.4 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
The study of LDHB (Lactate Dehydrogenase B) recombinant proteins has garnered significant attention due to their crucial role in metabolic pathways, particularly in the context of anaerobic glycolysis and lactate production. LDHB is a key enzyme that catalyzes the conversion of pyruvate to lactate, a process that is vital for cellular energy production under hypoxic conditions. Altered LDHB expression has been implicated in various diseases, including cancer, where it contributes to the Warburg effect—favoring glycolysis even in the presence of oxygen. As a result, understanding the structure and function of LDHB, along with its regulatory mechanisms, is crucial for elucidating its role in metabolic disorders and developing therapeutic interventions. Recombinant LDHB proteins enable researchers to investigate specific biochemical properties, enzyme kinetics, and interactions with various substrates or inhibitors. Furthermore, characterizing these proteins through techniques like X-ray crystallography and NMR can provide insights into the enzyme's active site and mechanisms of action. Overall, research on LDHB recombinant proteins not only enhances our comprehension of fundamental metabolic processes but also paves the way for novel strategies in treating conditions associated with dysregulated lactate metabolism, thereby highlighting the relevance of LDHB in both basic and clinical research settings.
