Analytical Data
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Gene name
PYK2
- Application
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Alternative Names
PYK2；NIR1；Membrane-associated phosphatidylinositol transfer Protein 3
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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
Q14289
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Expression Region
682-871aa
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AA Sequence
VYQMEKDIAMEQERNARYRTPKILEPTAFQEPPPKPSRPKYRPPPQTNLL APKLQFQVPEGLCASSPTLTSPMEYPSPVNSLHTPPLHRHNVFKRHSMRE EDFIQPSSREEAQQLWEAEKVKMRQILDKQQKQMVEDYQWLRQEEKSLDP MVYMNDKSPLTPEKEVGYLEFTGPPQKPPRLGAQSIQPTA
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Molecular Weight
47 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
PYK2 (Proline-rich tyrosine kinase 2) is a non-receptor tyrosine kinase that plays a critical role in various cellular processes, including cell adhesion, migration, and signal transduction. Its involvement in these processes makes PYK2 a significant player in physiological and pathological conditions, such as cancer metastasis and neurological disorders. The regulation of PYK2 activity is mediated by several mechanisms, including phosphorylation and interaction with various proteins, highlighting its complexity in cellular signaling pathways. The need for detailed studies of PYK2 has prompted researchers to explore its structure and function through recombinant protein expression. By generating recombinant PYK2, scientists can investigate its enzymatic activity, binding interactions, and regulatory mechanisms in vitro. Understanding PYK2 at the molecular level is crucial for elucidating its role in signaling networks and its potential as a therapeutic target for diseases associated with dysregulated kinase activity. As research progresses, insights gained from recombinant PYK2 studies may contribute to novel strategies for drug development and interventions in conditions where PYK2 is implicated.
