Analytical Data
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Gene name
PEAK1
- Application
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Alternative Names
KIAA2002
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Species
Human
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Source
Baculovirus
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Tag
His;GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H792
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Expression Region
K1127-R1746
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Protein Length
Partial
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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
PEAK1, or Protein Enriched in A Kinase Domain 1, is a potential oncogene implicated in various cancers and is recognized for its role in cellular signaling pathways. Research into PEAK1 has intensified due to its involvement in promoting tumorigenesis and influencing cell proliferation, migration, and invasion. It acts as a scaffold protein, integrating multiple signaling cascades, particularly those associated with growth factor receptors and the cytoskeleton. Elevated levels of PEAK1 have been observed in several malignancies, correlating with poor prognostic outcomes and increased metastatic potential. Consequently, understanding PEAK1’s molecular mechanisms and its interactions with other proteins is crucial for elucidating its contributions to cancer biology. Researchers are particularly interested in the development of PEAK1 inhibitors as targeted therapies, aiming to disrupt its function and ultimately impede tumor progression. Additionally, the exploration of PEAK1’s role in normal physiological processes offers insights into its dual functions in health and disease. Overall, the study of PEAK1 as a recombinant protein presents significant potential not only for therapeutic interventions but also for advancing our fundamental understanding of cancer biology and signaling network dynamics.
