Analytical Data
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Gene name
ldh1
- Application
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Alternative Names
ldh1；Laforin
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Species
E.coli
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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
P38139
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Expression Region
1-375aa
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AA Sequence
MNMAERAEATKSWSCEPLSGKTLEEIVQNAENAADLVAYIRKPEVDLDFRLKFIAEHEEFFNVQLSDRNSRIRTCHNLSDKGIRGDTVFVFVPGLAGNLEQFEPLLELVDSDQKAFLTLDLPGFGHSSEWSDYPMLKVVELIFVLVCDVLRKWSTAVPNNDNVNPFNGHKIVLVGHSMGCFLACHLYEQHMADTKAVQTLVLLTPPKAHIEQLSKDKHIIQWALYGVFKLPWLFDVYRNKFDQVKGLQSSGIKQYFYQQGDDVKLKYRKFWQFKNNISNKSRTIIGYLLGWETVDWVKFNGVLTQTDMKQKIIIFGAEKDPIAPIENLEFYKQTINKECLRKVIILPDCSHNLCFDRPELVCENFQREVIDNSKL
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Molecular Weight
43.2 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
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Protein Description
Lactate dehydrogenase (LDH) is an important enzyme involved in the metabolic process of converting lactate to pyruvate and vice versa, playing a critical role in anaerobic respiration and energy production. Among its five isoforms, LDH1 is predominantly expressed in the heart and red blood cells, making it a key player in cardiac metabolism and a potential biomarker for myocardial injury. Due to its significance in clinical diagnostics, researchers have focused on the recombinant production of LDH1 in various expression systems. The recombinant LDH1 protein allows for detailed studies of its enzymatic properties, structural characteristics, and interactions with other biomolecules. This research is pivotal in understanding the enzyme’s role in physiological and pathological conditions, including ischemic heart disease and cancer metabolism, as altered LDH activity is often associated with tumor progression and poor prognosis. Furthermore, the availability of purified recombinant LDH1 facilitates the development of therapeutic strategies and the exploration of its potential as a drug target. Understanding the mechanisms that regulate LDH1 activity could lead to innovative approaches in treating diseases associated with metabolic dysregulation. Thus, the study of recombinant LDH1 protein not only enhances our fundamental knowledge of metabolic pathways but also underscores its clinical relevance in biomarker development and therapeutic intervention.
