Analytical Data
-
Gene name
MIg
- Application
-
Alternative Names
MIg;MIG6;ERBB receptor feedback inhibitor 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P83881
-
Expression Region
1-106aa
-
AA Sequence
MVNVPKTRRT FCKKCGKHQP HKVTQYKKGK DSLYAQGKRR YDRKQSGYGG QTKPIFRKKA KTTKKIVLRL ECVEPNCRSK RMLAIKRCKH FELGGDKKRK GQVIQF
-
Molecular Weight
12.4 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
The study of MIg recombinant proteins stems from the growing need to understand and manipulate immune responses for therapeutic purposes. MIg, or "Monoclonal Immunoglobulin," plays a critical role in both the innate and adaptive immune systems, facilitating recognition and neutralization of pathogens. Recent advancements in biotechnology have enabled the production of MIg as recombinant proteins, allowing researchers to investigate their structure, function, and potential applications in immunotherapy and vaccine development. The ability to produce MIg in a controlled environment not only enhances our understanding of immune mechanisms but also paves the way for developing novel treatments for autoimmune diseases, cancers, and infectious diseases. As the field of immunology continues to evolve, the exploration of MIg recombinant proteins becomes increasingly significant, with potential implications for improving patient outcomes through targeted therapies and personalized medicine approaches. This research not only contributes to basic scientific knowledge but also holds promise for transformative healthcare solutions.











