Analytical Data
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Gene name
LDHAL6A
- Application
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Alternative Names
LDHAL6A; LDHL2L-lactate dehydrogenase A-like 6A; EC 1.1.1.27
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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
Q6ZMR3
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Expression Region
1-332aa
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AA Sequence
MATIKSELIK NFAEEEAIHH NKISIVGTGS VGVACAISIL LKGLSDELVL VDVDEGKLKG ETMDLQHGSP FMKMPNIVSS KDYLVTANSN LVIITAGARQ KKGETRLDLV QRNVSIFKLM IPNITQYSPH CKLLIVTNPV DILTYVAWKL SGFPKNRVIG SGCNLDSARF RYFIGQRLGI HSESCHGLIL GEHGDSSVPV WSGVNIAGVP LKDLNPDIGT DKDPEQWENV HKKVISSGYE MVKMKGYTSW GISLSVADLT ESILKNLRRV HPVSTLSKGL YGINEDIFLS VPCILGENGI TDLIKVKLTL EEEACLQKSA ETLWEIQKEL KL
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Molecular Weight
36.5 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
LDHAL6A (L-lactate dehydrogenase, on the other hand, was identified as a critical enzyme implicated in the oxidation of lactate to pyruvate, a key step in metabolic pathways relevant to cellular respiration and energy production. The protein has garnered interest due to its potential roles in various physiological and pathological processes, including cancer metabolism and tissue oxygenation. Preliminary studies suggest that LDHAL6A may play a role in regulating lactate levels and thus influence the tumor microenvironment and cancer cell proliferation. Given the increasing evidence linking altered lactate metabolism to various diseases, including metabolic disorders and cancers, researchers have begun exploring LDHAL6A as a potential therapeutic target or biomarker. The production of recombinant LDHAL6A protein allows for detailed biochemical analyses and structural studies, facilitating the understanding of its function and regulation. Additionally, studying the enzyme's activity and interactions with other metabolic pathways could provide insights into developing targeted therapies or diagnostic tools. Consequently, LDHAL6A is positioned as a promising candidate for further investigation in translational research aimed at addressing metabolic disruptions in cancer and other diseases. The ongoing research efforts focus on characterizing the recombinant protein's activity, stability, and potential interactions, which could ultimately contribute to novel therapeutic approaches in the fight against metabolic-related diseases.
