Analytical Data
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Gene name
V48C,L55C,R81P,N91S,S99N,T179P
- Application
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Alternative Names
(Protein FimH)
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Species
Escherichia coli
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08191
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Expression Region
22-180aa(V48C,L55C,R81P,N91S,S99N,T179P)
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Molecular Weight
18.4 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
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Protein Description
The recombinant proteins V48C, L55C, R81P, N91S, S99N, and T179P have garnered interest in the field of protein engineering and structural biology due to their potential applications in therapeutics and biocatalysis. These mutations have been identified in various biological contexts, suggesting their roles in altering protein stability, folding, and function. For instance, cysteine substitutions like V48C and L55C may enhance the formation of disulfide bonds, which can stabilize protein structures, while the proline substitution at R81P may introduce kinks in the polypeptide chain that affect its conformation. The other mutations, N91S, S99N, and T179P, may influence enzymatic activity or binding affinity by modifying critical residues involved in substrate interaction or maintaining the protein's active site. Understanding how these specific mutations impact the overall properties of the proteins can provide insights into the mechanisms of action for proteins involved in various biological processes. Furthermore, characterizing these recombinant proteins can lead to advances in synthetic biology, where engineered proteins can be tailored for specific functions, paving the way for innovative treatments and biotechnological applications. Collectively, the research on these mutants helps to elucidate the intricate relationship between sequence, structure, and function in proteins, which is essential for both fundamental science and applied research in biomedicine.
