Analytical Data
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Gene name
KRS
- Application
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Alternative Names
ATP13A2;PARK9;Polyamine-transporting ATPase 13A2
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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
Q15046
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Expression Region
63-597aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSGVGPEEESVDPNQYYKIRSQAIHQLKV NGEDPYPHKFHVDISLTDFIQKYSHLQPGDHLTDITLKVAGRIHAKRASG GKLIFYDLRGEGVKLQVMANSRNYKSEEEFIHINNKLRRGDIIGVQGNPG KTKKGELSIIPYEITLLSPCLHMLPHLHFGLKDKETRYRQRYLDLILNDF VRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAVAKPFITYHNE LDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDLTHNPEFTTCE FYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPEGQAYDVDFTP PFRRINMVEELEKALGMKLPETNLFETEETRKILDDICVAKAVECPPPRT TARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSKEGLTERFELF VMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFIDENFCTALEY GLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMKPEDKKENVATTDTLE STTVGTSV
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Molecular Weight
64 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
KRS, or L-lysine-α-ketoglutarate reductase, is an important enzyme involved in the metabolic pathways of amino acids and is significant for various biological processes. The study of KRS-recombinant proteins has garnered attention due to its potential applications in biotechnology and medicine. Recombinant protein technology, which involves the expression of proteins in heterologous systems, allows for the production of pure, active forms of KRS for detailed biochemical studies. Research on KRS has implications in understanding metabolic disorders, as it plays a crucial role in regulating the levels of specific metabolites in the body. Additionally, KRS has been associated with various diseases, including certain cancers, making its study critical for therapeutic targets. By investigating the structure and function of KRS through recombinant approaches, researchers aim to characterize its activity, optimize its enzymatic properties, and explore its interactions with other metabolic pathways. The production of KRS as a recombinant protein not only facilitates fundamental research but also paves the way for potential industrial applications, such as the development of biocatalysts for synthetic biology. Overall, exploring KRS-recombinant proteins provides valuable insights into metabolic regulation and opens new avenues for therapeutic interventions and biotechnological innovations.
