Analytical Data
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Gene name
LIPF
- Application
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Alternative Names
LIPF；Gastric triacylglycerol lipase
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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
P07098
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Expression Region
20-398aa
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AA Sequence
LFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPNLIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK
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Molecular Weight
50.1 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
Related Products
Protein Description
LIPF, or Lipoprotein Lipase-Related Protein, is a member of the lipase family that plays a crucial role in lipid metabolism and homeostasis. Investigating LIPF is of significant interest due to its involvement in various physiological processes and its potential implications in metabolic disorders. Originally identified for its role in hydrolyzing triglycerides, LIPF has garnered attention for its functions beyond lipid metabolism, including its regulatory effects on inflammation and cardiovascular health. Recent studies suggest that altered LIPF expression may contribute to diseases such as obesity, diabetes, and atherosclerosis, highlighting the importance of understanding its mechanisms at both molecular and physiological levels. Furthermore, LIPF's interactions with other proteins and its expression patterns in different tissues provide valuable insights into its multifaceted roles in cellular processes. As researchers continue to explore LIPF's biological functions, the development of LIPF recombinants for experimental purposes has become a crucial step. These recombinant proteins facilitate the study of LIPF's enzymatic properties, interactions, and regulatory mechanisms in vitro and in vivo. Elucidating the structure-function relationship of LIPF could lead to novel therapeutic strategies targeting metabolic diseases, thereby underscoring the significance of ongoing research in this field. Overall, understanding LIPF and its pathways presents a promising avenue for advancing our knowledge of lipid metabolism and its associated health implications.
