Analytical Data
-
Gene name
Elastase
- Application
-
Species
Salmo salar
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q7SIG3
-
Expression Region
1-236aa
-
Molecular Weight
31.0 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
Elastase is a serine protease primarily produced by neutrophils and plays a crucial role in the degradation of elastin and other extracellular matrix components. Its dysregulation is linked to various pathological conditions, such as emphysema, rheumatoid arthritis, and chronic obstructive pulmonary disease (COPD). Given its significant role in tissue remodeling and inflammation, elastase has become a target for therapeutic interventions. Research on recombinant elastase has gained traction, allowing for the production of this enzyme with specific mutations or modifications that enhance its stability and activity. Advances in genetic engineering, particularly with the use of techniques like CRISPR and various expression systems, have facilitated the generation of recombinant elastase for both basic research and potential clinical applications. By studying its structure and function, scientists aim to decipher the enzyme's precise mechanisms in disease processes, paving the way for the development of inhibitors that could mitigate its detrimental effects. Overall, recombinant elastase research not only contributes to our understanding of proteolytic enzymes in health and disease but also holds promise for innovative therapeutic strategies.
