Analytical Data
-
Gene name
IgJ
- Application
-
Alternative Names
Jchain; IgjImmunoglobulin J chain
-
Species
Mouse
-
Source
Yeast
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P01592
-
Expression Region
22-159aa
-
Molecular Weight
17.7 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
Identification
Protein Description
The study of FCAR (Fc alpha receptor) and CD89 (CD89 antigen) recombinant proteins has gained significant attention in immunology and therapeutic research due to their roles in the immune response. FCAR is a cell surface receptor predominantly expressed on myeloid cells, facilitating the interaction between IgA-bound pathogens and immune cells, thus enhancing immune responses. CD89, as the receptor for IgA, plays a crucial role in mediating IgA antibody-dependent cellular phagocytosis and inflammation, contributing to the body’s defense mechanisms against infections. Understanding the structure and function of FCAR/CD89 recombinant proteins can provide insights into their signaling pathways and interaction with pathogens. This knowledge is essential for developing novel immunotherapeutic strategies for treating diseases where immune regulation is compromised, such as autoimmune disorders and infections. Additionally, the production of these recombinant proteins allows for detailed studies on receptor-ligand interactions, which can reveal potential targets for drug development. Overall, the characterization of FCAR/CD89 recombinant proteins holds promise for advancing our understanding of immune responses and creating innovative therapeutic interventions.











