Analytical Data
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Gene name
LMF2
- Application
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Alternative Names
TMEM153; TMEM112B; Transmembrane Protein 153
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BU23
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Expression Region
Leu454~Lys707
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Molecular Weight
33kDa
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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
LMF2 (Lipid Metabolism Factor 2) is a protein that has gained attention in recent years due to its critical role in lipid metabolism and its implications for various metabolic disorders. Research indicates that LMF2 is involved in the regulation of triacylglycerol and phospholipid biosynthesis, playing a significant part in maintaining cellular lipid homeostasis. Abnormalities in lipid metabolism are linked to conditions such as obesity, diabetes, and cardiovascular diseases, making LMF2 a potential target for therapeutic interventions. The characterization of LMF2 through recombinant protein studies allows researchers to gain deeper insights into its functional properties and regulatory mechanisms. Moreover, the availability of LMF2 as a recombinantly expressed protein provides a valuable tool for studying its interactions with other lipid metabolic pathways and proteins, facilitating the exploration of novel strategies to modulate its activity for treating metabolic disorders. Hence, understanding LMF2's structure, function, and interaction with cellular systems is essential for elucidating its role in health and disease, and for the potential development of targeted therapies to address lipid-related pathologies.
