Analytical Data
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Gene name
LIPB
- Application
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Alternative Names
LIPB；Lipoyl amidotransferase LIPT1. mitochondrial
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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
Q9Y234
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Expression Region
1-373aa
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AA Sequence
MLIPFSMKNCFQLLCNCQVPAAGFKKTVKNGLILQSISNDVYQNLAVEDWIHDHMNLEGKPILFFWQNSPSVVIGRHQNPWQECNLNLMREEGIKLARRRSGGGTVYHDMGNINLTFFTTKKKYDRMENLKLIVRALNAVQPQLDVQATKRFDLLLDGQFKISGTASKIGRTTAYHHCTLLCSTDGTFLSSLLKSPYQGIRSNATASIPSLVKNLLEKDPTLTCEVLMNAVATEYAAYHQIDNHIHLINPTDETLFPGINSKAKELQTWEWIYGKTPKFSINTSFHVLYEQSHLEIKVFIDIKNGRIEICNIEAPDHWLPLEIRDKLNSSLIGSKFCPTETTMLTNILLRTCPQDHKLNSKWNILCEKIKGIM
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Molecular Weight
42.4 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
Related Products
Protein Description
LIPB, or Lipase B, is an enzyme known for its role in lipid metabolism and has garnered considerable interest in recent years due to its potential applications in biotechnology and medicine. Research on LIPB focuses on its ability to hydrolyze triglycerides and phospholipids, making it essential for various physiological processes, including fat digestion and energy homeostasis. The recombinant production of LIPB has become a prominent area of study, as it bypasses the limitations associated with natural enzyme extraction from sources like animal tissues or microorganisms. Researchers are exploring genetic engineering techniques to produce LIPB in host organisms such as bacteria and yeast, enabling the scaling of enzyme production for industrial use. This approach not only enhances the yield and purity of the enzyme but also allows for the modification of its properties to improve stability, activity, and substrate specificity. The advancements in LIPB research highlight its promising potential in diverse fields, including food processing, biocatalysis, and therapeutic applications, particularly in treating lipid-related disorders. The ongoing exploration of LIPB's structure-function relationships and its interaction with various substrates is contributing to a deeper understanding of lipid metabolism and facilitating the development of innovative biotechnological solutions.
