Analytical Data
-
Gene name
C114S,K127N
- Application
-
Alternative Names
(Odorant-binding protein IIa)(OBPIIa)
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9NY56
-
Expression Region
16-170aa(C114S,K127N)
-
Molecular Weight
30.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
The C114S and K127N mutants of a specific protein have garnered attention in the field of protein engineering and biochemistry due to their potential applications in therapeutic development and functional studies. The C114 residue is often crucial for the protein's structural stability and catalytic function, while the K127 position may play a role in substrate binding or protein-protein interactions. Studying these mutations allows researchers to elucidate the functional importance of these residues in the context of the protein's overall mechanism. The C114S mutation, which replaces cysteine with serine, is expected to affect disulfide bonding and potentially alter the protein's conformation, while the K127N mutation introduces a polarity change that could influence interactions within protein complexes. These findings are critical for advancing our understanding of the protein's biochemical properties and could inform the design of inhibitors or activators tailored for therapeutic use. Investigating the structural and functional implications of C114S and K127N not only enhances our comprehension of the target protein but also contributes to the broader field of protein design as scientists aim to develop novel proteins with improved stability and functionality for various biomedical applications.
