Analytical Data
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Gene name
lplA
- Application
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Alternative Names
lplA；yjjF；Lipoate-Protein ligase A
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Species
E.coli
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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
C4ZT68
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Expression Region
1-338aa
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AA Sequence
MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPEQEKELRELSAWMAGAVR
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Molecular Weight
53.9 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
LplA, or Lipase A, is an extracellular enzyme predominantly produced by various bacterial species, including those belonging to the genus *Pseudomonas*. Its role in lipid metabolism has garnered significant interest due to its potential applications in biotechnological processes, such as biodiesel production, food industry, and bioremediation. The ability of LplA to efficiently hydrolyze triglycerides offers opportunities for enhancing the efficiency of lipid conversion processes. The recombinant expression of LplA, through leveraging various expression systems, allows researchers to produce this enzyme in a controlled and scalable manner. This enables detailed studies of its biochemical properties, substrate specificity, and catalytic mechanisms. Additionally, the functional characterization of LplA can facilitate the design of engineered enzymes with improved performance for industrial applications. Understanding the structure-function relationship of LplA through techniques like X-ray crystallography and mutagenesis studies can lead to insights that optimize its use in various fields, thereby promoting sustainable practices in energy production and environmental management.
