Analytical Data
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Gene name
LDHAL6B
- Application
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Alternative Names
LDHAL6B; LDHAL6; LDHLL-lactate dehydrogenase A-like 6B; EC 1.1.1.27
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BYZ2
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Expression Region
1-381aa
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AA Sequence
MSWTVPVVRASQRMSSVGANFLCLGMALCLRQATRIPLNGTWLFTPVSKMATVKSELIERFTSEKPVHHSKVSIIGTGSVGMACAISILLKGLSDELALVDLDEDKLKGETMDLQHGSPFTKMPNIVCSKDYFVTANSNLVIITAGARQEKGETRLNLVQRNVAIFKLMISSIVQYSPHCKLIIVSNPVDILTYVAWKLSAFPKNRIIGSGCNLDTARFRFLIGQKLGIHSESCHGWILGEHGDSSVPVWSGVNIAGVPLKDLNSDIGTDKDPEQWKNVHKEVTATAYEIIKMKGYTSWAIGLSVADLTESILKNLRRIHPVSTITKGLYGIDEEVFLSIPCILGENGITNLIKIKLTPEEEAHLKKSAKTLWEIQNKLKL
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Molecular Weight
68.4 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
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Protein Description
LDHAL6B (L-lactate dehydrogenase-like 6B) is a recently identified protein that plays a significant role in cellular metabolism and various physiological processes. Emerging evidence suggests that LDHAL6B is involved in the regulation of lactate metabolism, which is crucial for energy production, especially in hypoxic conditions where cells rely on anaerobic glycolysis. Research has indicated that aberrations in LDHAL6B expression may be linked to metabolic disorders and certain types of cancer, highlighting its potential as a biomarker for disease states. Furthermore, studies have begun to explore its structural characteristics, enzymatic activities, and interactions with other metabolic pathways, which may provide deeper insights into its biological functions. The interest in LDHAL6B has also been fueled by its potential therapeutic implications, as modulating its activity could offer novel strategies for treating metabolic diseases or enhancing cancer therapies. Overall, understanding LDHAL6B at the molecular level could pave the way for new approaches in medical research and drug development, making it a promising target for future studies.
