Analytical Data
-
Gene name
AF1521
- Application
-
Alternative Names
AF_1521
-
Species
Pan-species (General)
-
Source
E. coli
-
Tag
Two N- s, His- & SUMO-
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O28751
-
Expression Region
Met1~Leu192
-
Molecular Weight
38kDa
-
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
AF1521 is a recombinant protein derived from a specific bacterial strain, which has garnered attention due to its potential therapeutic applications and role in various biochemical processes. The research background of AF1521 is rooted in the growing need for efficient proteins that can be used in drug development, diagnostics, and biotechnological applications. Studies have indicated that AF1521 may possess unique properties that enable it to exhibit significant biological activity, making it a candidate for further exploration in functional assays and structural biology. The protein's ability to interact with cellular pathways and its stability make it a promising target for the development of new therapies aimed at treating various diseases, including metabolic disorders and infectious diseases. Researchers are focusing on elucidating the protein's mechanism of action, optimizing expression systems for large-scale production, and characterizing its structure-function relationship. Overall, the investigation of AF1521 not only advances our understanding of recombinant protein technology but also enhances the potential for novel clinical applications.
