Analytical Data
-
Gene name
R294C
- Application
-
Alternative Names
Serpin C1
-
Species
Human
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P01008
-
Expression Region
1-464aa(R294C)
-
Molecular Weight
58.5 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 R294C mutant of a specific protein has garnered attention in recent research due to its implications in understanding disease mechanisms and protein functionality. This mutation, occurring at the 294th residue where arginine is replaced by cysteine, is often associated with various genetic disorders, including certain forms of cardiomyopathy and other metabolic conditions. Studies indicate that such mutations can disrupt normal protein folding and stability, leading to altered biological activity. Researchers utilize recombinant protein technology to produce the R294C variant, enabling detailed biophysical and biochemical analyses. These studies aim to elucidate how this mutation affects the protein's interactions, structural integrity, and overall role in cellular pathways. Furthermore, understanding the consequences of this particular mutation can provide insights into potential therapeutic targets and strategies for treating associated disorders. By characterizing the R294C variant, scientists hope to advance the knowledge of mutation-driven disease mechanisms and contribute to the development of gene therapies or small-molecule drugs designed to counteract the effects of this and similar mutations.
