Analytical Data
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Gene name
PTK9L
- Application
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Alternative Names
PTK9L
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Species
Human
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6IBS0
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Expression Region
M1-S349
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Protein Length
Full Length
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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
PTK9L (also known as PTK9-like) is a member of the protein tyrosine kinase family, which plays a crucial role in various cellular processes, including signal transduction, cell growth, adhesion, and differentiation. Research into PTK9L has gained interest due to its potential involvement in several pathological conditions, including cancer and neurodegenerative diseases. The understanding of PTK9L's function and its molecular mechanisms could provide insights into tumorigenesis and cellular signaling pathways. Additionally, PTK9L has been implicated in supporting cellular responses to stress and promoting survival under adverse conditions, making it a relevant target for therapeutic interventions. Recombinant protein studies of PTK9L enable the exploration of its biochemical properties, interactions with other signaling molecules, and its role in disease mechanisms. This research can also lead to the development of novel pharmacological approaches aimed at modulating its activity, which could prove beneficial in treating diseases where PTK9L is dysregulated. Overall, the investigation of PTK9L recombinant proteins is vital for elucidating their roles in health and disease, paving the way for future biomedical applications.
