Analytical Data
-
Gene name
IkBb
- Application
-
Alternative Names
IkBb；IKBB；TRIP9；NF-kappa-B inhibitor beta
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q15653
-
Expression Region
1-356aa
-
AA Sequence
MAGVACLGKA ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPGLSWAPLV FGYVTEDGDT ALHLAVIHQH EPFLDFLLGF SAGTEYMDLQ NDLGQTALHL AAILGETSTV EKLYAAGAGL CVAERRGHTA LHLACRVGAH ACARALLQPR PRRPREAPDT YLAQGPDRTP DTNHTPVALY PDSDLEKEEE ESEEDWKLQL EAENYEGHTP LHVAVIHKDV EMVRLLRDAG ADLDKPEPTC GRSPLHLAVE AQAADVLELL LRAGANPAAR MYGGRTPLGS AMLRPNPILA RLLRAHGAPE PEGEDEKSGP CSSSSDSDSG DEGDEYDDIV VHSSRSQTRL PPTPASKPLP DDPRPV
-
Molecular Weight
37.7 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
Protein Description
The study of IkBβ recombinant protein has garnered significant attention due to its pivotal role in regulating the NF-κB signaling pathway, which is crucial for various cellular processes including inflammation, immune response, and cell survival. IkBβ functions as an inhibitor of NF-κB, sequestering it in the cytoplasm and preventing its nuclear translocation and subsequent transcriptional activity. Dysregulation of this pathway is implicated in a range of diseases, including cancer, autoimmune disorders, and chronic inflammatory conditions. By producing and characterizing IkBβ recombinant protein, researchers aim to elucidate its structural and functional properties, which can provide insights into its mechanism of action and potential therapeutic applications. Recombinant protein techniques allow for the generation of sufficient quantities of active IkBβ, enabling detailed biochemical assays and structural analyses. This research not only enhances our understanding of NF-κB regulation but also opens up possibilities for developing novel drugs targeting this pathway, thereby contributing to more effective treatments for conditions associated with its dysregulation. Furthermore, studying IkBβ interactions with other cellular proteins may reveal new regulatory mechanisms and pathways, highlighting its importance as a potential therapeutic target in inflammatory and oncogenic processes.
