Analytical Data
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Gene name
Lipoate-protein ligase A/LplA
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简介
Lipoic acid protein ligase A (LplA) is a key enzyme involved in the activation and transfer of lipoic acid, an important cofactor, to the lipoyl domain of lipoic acid-dependent enzymes. LplA catalyzes the ATP-dependent activation of exogenous lipoic acid, converting it to lipoyl-AMP as an intermediate. Lipoate-protein ligase A/LplA Protein, E.coli (His-SUMO) is the recombinant E. coli-derived Lipoate-protein ligase A/LplA protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag.
- Application
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Alternative Names
lplA; BWG_4078Lipoate-protein ligase A; EC 6.3.1.20; Lipoate--protein ligase
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Species
E.coli
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Source
E. coli
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Tag
N-SUMO;N-6*His
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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
M1-R338
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AA Sequence
MSTLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKTISTSIVLNALNALGVSAEASGRNDLVVKTVEGDRKVSGSAYRETKDRGFHHGTLLLNADLSRLANYLNPDKKKLAAKGITSVRSRVTNLTELLPGITHEQVCEAITEAFFAHYGERVEAEIISPNKTPDLPNFAETFARQSSWEWNFGQAPAFSHLLDERFTWGGVELHFDVEKGHITRAQVFTDSLNPAPLEALAGRLQGCLYRADMLQQECEALLVDFPEQEKELRELSAWMAGAVR
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Protein Length
Full Length
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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
Lipoate-protein ligase A (LplA) plays a crucial role in the post-translational modification of proteins by catalyzing the attachment of lipoate, a bioactive lipid cofactor, to specific lysine residues on target proteins. This modification is essential for the proper functioning of several key enzymes involved in mitochondrial metabolism, including those in the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes. Given its significance, LplA has garnered attention in the field of biochemistry and molecular biology, with researchers investigating its structure, mechanism, and potential applications. The ability to produce recombinant LplA in sufficient quantities allows for detailed functional studies and the development of assays to screen for inhibitors that could modulate its activity, thereby providing insights into metabolic diseases associated with dysfunctional lipoic acid metabolism. Additionally, understanding LplA has implications for biotechnology, particularly in the development of novel therapeutics that exploit lipoate attachment for enhancing protein function or stability. Overall, the study of LplA not only illuminates fundamental biological processes but also opens avenues for innovative solutions in medicine and industry.
