Analytical Data
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Gene name
KDSR
- Application
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Alternative Names
KDSR;FVT1;SDR35C1;3-ketodihydrosphingosine reductase
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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
Q06136
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Expression Region
26-270aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMKPLALPGAHVVVTGGSSGIGKCIAIECYK QGAFITLVARNEDKLLQAKKEIEMHSINDKQVVLCISVDVSQDYNQVENV IKQAQEKLGPVDMLVNCAGMAVSGKFEDLEVSTFERLMSINYLGSVYPSR AVITTMKERRVGRIVFVSSQAGQLGLFGFTAYSASKFAIRGLAEALQMEV KPYNVYITVAYPPDTDTPGFAEENRTKPLETRLISETTSVCKPEQVAKQI VKDAIQGNFNSSLGSD
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Molecular Weight
29 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
KDSR (2-keto-3-deoxy-D-manno-octulosonic acid reductase) is an enzyme involved in the biosynthesis of lipopolysaccharides (LPS), which are crucial components of the outer membrane of Gram-negative bacteria. The research on KDSR has gained significant attention due to its role in bacterial pathogenesis and its potential as a target for antimicrobial drug development. LPS plays a pivotal role in the structural integrity of the bacterial cell and mediates interactions with the host immune system. Understanding the structure and function of KDSR is essential for elucidating its mechanism in LPS biosynthesis. Moreover, the reconstitution of KDSR in a laboratory setting allows for detailed biochemical analysis, enabling researchers to explore its catalytic properties and interactions with substrates and inhibitors. By manipulating KDSR, scientists aim to develop novel therapeutic strategies to combat antibiotic-resistant infections posed by Gram-negative bacteria. Additionally, characterizing the restructured KDSR protein can provide insights into enzyme engineering and synthetically altering pathways in bacterial metabolism, which could have broader implications in biotechnology and synthetic biology. Overall, the study of KDSR not only furthers our understanding of microbial physiology but also represents a promising avenue for innovative approaches in antibiotic design and drug development.
