Analytical Data
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Gene name
GSK3
- Application
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Alternative Names
GSK3;Glycogen synthase kinase-3 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
P49841
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Expression Region
1-420aa
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AA Sequence
MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF NFTTQELSSN PPLATILIPP HARIQAAAST PTNATAASDA NTGDRGQTNN AASASASNST HHHHHH
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Molecular Weight
48 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
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Protein Description
Glycogen synthase kinase 3 (GSK3) is a serine/threonine kinase that plays a critical role in various cellular processes, including glycogen metabolism, cell differentiation, and apoptosis. It exists in two isoforms, GSK3α and GSK3β, both of which are highly conserved across species and are implicated in numerous signaling pathways, particularly those involving insulin and Wnt. Dysregulation of GSK3 has been associated with several diseases, including diabetes, cancer, and neurodegenerative disorders such as Alzheimer’s disease. The study of recombinant GSK3 proteins has become increasingly important for elucidating the structure-function relationships of this kinase and understanding its regulatory mechanisms. By producing and characterizing recombinant GSK3, researchers can explore its enzymatic activity, substrate specificity, and interactions with other proteins, which are critical for developing therapeutic strategies that target GSK3 pathways. The insights gained from such studies may lead to the discovery of small-molecule inhibitors or other modulators that could be beneficial in treating diseases where GSK3 is a pivotal player. Furthermore, the availability of recombinant GSK3 also facilitates high-throughput screening assays, aiding in the identification of potential drug candidates. Overall, research on recombinant GSK3 proteins not only enhances our fundamental understanding of cellular signaling but also holds significant promise for the advancement of targeted therapies in various pathologies.
