Analytical Data
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Gene name
LPIN1
- Application
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Alternative Names
Phosphatidate phosphatase LPIN1
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Species
Rat
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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
Q5XIM8
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Expression Region
Thr729~Ala924
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Molecular Weight
26kDa
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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
LPIN1 (lipin-1) is a crucial protein involved in lipid metabolism, and its study has garnered significant attention due to its role in energy homeostasis and cellular signaling. The LPIN1 gene encodes for a phosphatidic acid phosphatase enzyme that catalyzes the dephosphorylation of phosphatidic acid to diacylglycerol, a key step in the biosynthesis of triglycerides and phospholipids. Mutations or dysregulation of LPIN1 have been linked to metabolic disorders, including obesity, insulin resistance, and fatty liver disease. Researchers have been interested in recombinant LPIN1 proteins to better understand its structure-function relationship, regulatory mechanisms, and interactions with other proteins involved in lipid metabolism. By producing LPIN1 as a recombinant protein, scientists can perform in vitro studies to elucidate its enzymatic activity, explore its role in lipid storage and mobilization, and investigate how altered LPIN1 function contributes to metabolic dysregulation. The insights gained from studying recombinant LPIN1 could provide new therapeutic targets for treating metabolic diseases and improving conditions associated with lipid metabolism disorders. Hence, the research on LPIN1 recombinant protein is paramount for advancing our understanding of metabolic pathways and developing potential interventions for related health issues.
