Analytical Data
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Gene name
PRKD1
- Application
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Alternative Names
PRKD1; PRK-D1; PKC-MU; PKCM; PK-D1; PRKCM; Protein Kinase C,Mu
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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 95% as determined by SDS-PAGE.
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Uniprot
Q15139
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Expression Region
Thr651~Gln876
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Molecular Weight
32kDa
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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
PRKD1, or Protein Kinase D1, is a serine/threonine kinase that plays a crucial role in a variety of cellular processes, including cell proliferation, differentiation, and apoptosis. Its dysregulation has been implicated in several diseases, particularly in cancer, where it may affect tumor growth and metastasis. The study of PRKD1 has gained attention due to its involvement in key signaling pathways, such as those mediated by phorbol esters and other mitogenic signals, which are essential for cellular responses to growth factors and stress. Recent research has focused on the structural and functional characterization of PRKD1 and its potential as a therapeutic target. Researchers have employed recombinant protein techniques to produce active PRKD1, allowing for detailed investigation of its enzymatic properties, substrate specificity, and interactions with other signaling molecules. Understanding the precise mechanisms by which PRKD1 contributes to cellular dysfunction could pave the way for novel therapeutic strategies aimed at modulating its activity in disease contexts, particularly in oncological applications where PRKD1 activity might influence tumor dynamics.
