Analytical Data
-
Gene name
IgG
- Application
-
Alternative Names
IgG；FCRN；IgG receptor FcRn large subunit p51
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P55899
-
Expression Region
24-297aa
-
AA Sequence
AESHLSLLYHLTAVSSPAPGTPAFWVSGWLGPQQYLSYNSLRGEAEPCGAWVWENQVSWYWEKETTDLRIKEKLFLEAFKALGGKGPYTLQGLLGCELGPDNTSVPTAKFALNGEEFMNFDLKQGTWGGDWPEALAISQRWQQQDKAANKELTFLLFSCPHRLREHLERGRGNLEWKEPPSMRLKARPSSPGFSVLTCSAFSFYPPELQLRFLRNGLAAGTGQGDFGPNSDGSFHASSSLTVKSGDEHHYCCIVQHAGLAQPLRVELESPAKSS
-
Molecular Weight
57.4 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
Immunoglobulin G (IgG) is a crucial antibody type in the immune response, primarily responsible for identifying and neutralizing pathogens such as bacteria and viruses. The study of recombinant IgG proteins has gained significant traction in biomedical research and therapeutic development. This interest is driven by the need for specific and effective treatments, including monoclonal antibodies that can precisely target diseases like cancer, autoimmune disorders, and infectious diseases. Advances in recombinant DNA technology enable the production of engineered IgG proteins with tailored properties, enhancing their efficacy and safety profiles. Furthermore, recombinant IgG can be produced at scale in various expression systems, including bacterial, yeast, and mammalian cells, facilitating large-scale production for clinical use. Research in this area also explores the structural and functional modifications of IgG, such as Fc-engineering to improve half-life or enhance effector functions, which can lead to superior therapeutic outcomes. Overall, the development and application of recombinant IgG proteins represent a dynamic field with the potential to revolutionize modern medicine and improve patient care.
