Analytical Data
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Gene name
IkBa
- Application
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Alternative Names
IkBa；IKBA；MAD3；NFKBI；NF-kappa-B inhibitor alpha
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P25963
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Expression Region
1-317aa
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AA Sequence
MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ EIRLEPQEVP RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD LAFLNFQNNL QQTPLHLAVI TNQPEIAEAL LGAGCDPELR DFRGNTPLHL ACEQGCLASV GVLTQSCTTP HLHSILKATN YNGHTCLHLA SIHGYLGIVE LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG ADVNRVTYQG YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE DELPYDDCVF GGQRLTL
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Molecular Weight
35.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
IkBa (Inhibitor of Nuclear Factor kappa B alpha) is a crucial protein involved in the regulation of the NF-κB signaling pathway, which plays a pivotal role in immune responses, inflammation, and cell survival. Dysregulation of this pathway is associated with various diseases, including cancers and autoimmune disorders. Research on IkBa has gained momentum due to its potential as a therapeutic target; specifically, the manipulation of its expression and function may offer novel approaches for treating related diseases. The study of recombinant IkBa proteins has become essential for understanding their structure-function relationships and for elucidating the molecular mechanisms by which they regulate NF-κB activity. Recombinant technology allows for the production of high-purity IkBa proteins, enabling comprehensive functional assays and structural analyses. These studies can help identify key domains responsible for protein interactions, post-translational modifications, and mechanisms of inhibition. Moreover, understanding diverse isoforms and the impact of mutations on IkBa function could reveal critical insights into its role in disease pathology. Overall, the research into recombinant IkBa proteins holds significant promise for advancing our understanding of NF-κB signaling and developing targeted therapies for related diseases.
