Analytical Data
-
Gene name
IgG1
- Application
-
Alternative Names
IgG1;Fcgr3a;Low affinity immunoglobulin gamma Fc region receptor III-A
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P05112
-
Expression Region
25-153aa
-
AA Sequence
HKCDITLQEI IKTLNSLTEQ KTLCTELTVT DIFAASKNTT EKETFCRAAT VLRQFYSHHE KDTRCLGATA QQFHRHKQLI RFLKRLDRNL WGLAGLNSCP VKEANQSTLE NFLERLKTIM REKYSKCSS
-
Molecular Weight
15.0 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
IgG1 recombinant proteins have emerged as critical tools in the fields of biotechnology and medicine, primarily due to their significant role in the immune response and therapeutic applications. Immunoglobulin G (IgG) is the most abundant antibody isotype in serum and plays a key role in pathogen neutralization and opsonization. The study of IgG1, in particular, has gained prominence as advancements in recombinant DNA technology allow for the production of high-affinity antibodies with tailored characteristics. This is particularly relevant for monoclonal antibodies (mAbs), which are increasingly used in targeted therapies for various diseases, including cancers and autoimmune disorders. Understanding the structure-function relationship of IgG1 enables researchers to enhance its stability, efficacy, and specificity against antigens. Additionally, modifications in the Fc region of IgG1 can improve its interaction with Fc receptors, thereby augmenting its potential for therapeutic use. As a result, research in IgG1 recombinant proteins not only supports the development of novel therapies but also provides insights into fundamental immunological processes, paving the way for innovative applications in diagnostics and treatment strategies. Furthermore, the growing interest in biopharmaceuticals underscores the importance of optimizing recombinant IgG1 production systems to ensure high yield and functionality, facilitating their use in clinical settings.











