Analytical Data
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Gene name
PTK6
- Application
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Alternative Names
BRK; Breast tumor kinase; Tyrosine-protein kinase BRK
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13882
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Expression Region
Phe191~Thr445
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Molecular Weight
33KDa
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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
PTK6, or protein tyrosine kinase 6, is a non-receptor tyrosine kinase that has garnered attention in cancer research due to its prominent role in cellular signaling and its association with various malignancies. Initially identified as a critical player in cellular proliferation and differentiation, PTK6 regulates multiple signaling pathways, including those related to cell survival and apoptosis. Its expression is prevalent in epithelial tissues, and dysregulation of PTK6 has been implicated in tumorigenesis, particularly in breast, prostate, and colorectal cancers. Researchers have observed that PTK6 can promote cancer cell migration and invasion, making it a potential target for therapeutic interventions. The investigation of recombinant PTK6 proteins aims to elucidate its functional mechanisms, domain interactions, and regulatory roles within cellular contexts. By studying PTK6 through recombinant expression systems, scientists can analyze its biochemical properties, domain architecture, and post-translational modifications, which may provide insights into its contribution to cancer progression and metastasis. Furthermore, understanding PTK6's interaction with other signaling molecules opens avenues for developing targeted therapies that could inhibit its oncogenic activity, ultimately contributing to more effective cancer treatment strategies.
