Analytical Data
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Gene name
STYK1
- Application
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Alternative Names
STYK1; NOK; Tyrosine-protein kinase STYK1; Novel oncogene with kinase domain; Protein PK-unique; Serine/threonine/tyrosine kinase 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6J9G0
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Expression Region
1-422 aa
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AA Sequence
MGMTRMLLECSLSDKLCVIQEKQYEVIIVPTLLVTIFLILLGVILWLFIREQRTQQQRSGPQGIAPVPPPRDLSWEAGHGGNVALPLKETSVENFLGATTPALAKLQVPREQLSEVLEQICSGSCGPIFRANMNTGDPSKPKSVILKALKEPAGLHEVQDFLGRIQFHQYLGKHKNLVQLEGCCTEKLPLYMVLEDVAQGDLLGFLWTCRRDVMTMDGLLYDLTEKQVYHIGKQVLLALEFLQEKHLFHGDVAARNILMQSDLTAKLCGLGLAYEVYTRGAISSTQTIPLKWLAPERLLLRPASIRADVWSFGILLYEMVTLGAPPYPEVPPTSILEHLQRRKIMKRPSSCTHTMYSIMKSCWRWREADRPSPRELRLRLEAAIKTADDEAVLQVPELVVPELYAAVAGIRVESLFYNYSML
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Molecular Weight
73.9 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
STYK1, also known as serine/threonine kinase 1, has emerged as a significant focus in cancer research due to its involvement in various cellular processes, including cell proliferation, differentiation, and apoptosis. Abnormal expression of STYK1 has been associated with several types of malignancies, which suggests its potential role as a biomarker for cancer progression and prognosis. Recent studies have illustrated that STYK1 functions as a signaling molecule that can modulate key pathways involved in tumorigenesis, notably the MAPK/ERK and PI3K/AKT pathways, thereby influencing cell cycle regulation and survival mechanisms in cancer cells. Furthermore, the overexpression of STYK1 has been linked to enhanced metastatic potential and resistance to therapeutic interventions, underscoring its importance in cancer biology. As a result, the development of STYK1 recombinant proteins has become a vital area of research, aiming to elucidate its precise biological functions and molecular mechanisms. These recombinant proteins can serve as valuable tools in dissecting the signaling pathways mediated by STYK1, aiding in the identification of potential therapeutic targets. Additionally, understanding STYK1’s interactions with other proteins within the cellular framework can provide insights into its role in disease progression, potentially leading to innovative approaches for cancer treatment and management. Overall, the study of STYK1 through recombinant protein technology holds promise not only for elucidating fundamental biological processes but also for advancing clinical applications in oncology.
