Analytical Data
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基因名
LDHB
- Application
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别名
LDHB；L-lactate dehydrogenase B chain
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P07195
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表达区间
2-334aa
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氨基酸序列
ATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL
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分子量
43.4 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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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.
