Analytical Data
-
Gene name
SI
- Application
-
Alternative Names
SI；SIAT10；Type 2 lactosamine alpha-2.3-sialyltransferase
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P14410
-
Expression Region
全长
-
AA Sequence
full
-
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 study of single-chain antibody fragments (scFvs) has gained significant traction in recent years due to their versatile applications in diagnostics and therapeutics. As a result of their smaller size compared to full-length antibodies, scFvs offer advantages such as improved tissue penetration, simpler production, and easier engineering for specific applications. Their modular nature allows researchers to link antibody variable regions, enabling the creation of tailored protein formats, which can be utilized in targeted drug delivery, cancer therapy, and as molecular tools for detecting biomolecules. Furthermore, advances in recombinant DNA technology have facilitated the efficient expression and purification of scFvs, paving the way for high-throughput screening methods that identify optimal candidates from vast libraries. This research not only addresses the challenges of traditional antibody production but also opens up new avenues for engineering proteins with enhanced stability and specificity. Consequently, the exploration of scFvs has become a pivotal area in biomedical research, with ongoing studies focusing on their optimization and application in various fields, including immunotherapy, vaccine development, and personalized medicine. Understanding the structural and functional dynamics of scFvs is essential for developing next-generation biotherapeutics that can effectively target a wide range of diseases.
