Analytical Data
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Gene name
DSTYK
- Application
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Alternative Names
RIPK5; Dusty PK; RIP5; SgK496; Receptor Interacting Protein Kinase 5; RIP-homologous kinase; Sugen kinase 496; Receptor-interacting serine/threonine-protein kinase 5
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Species
Rat
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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
Q6XUX2
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Expression Region
Pro650~Leu904
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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
Related Products
Protein Description
DSTYK (Dual-specificity tyrosine-phosphorylation-regulated kinase) is a dual-specificity protein kinase that has garnered attention in recent years due to its potential roles in various cellular processes and pathologies. This protein is implicated in the regulation of several critical signaling pathways, influencing cell proliferation, differentiation, and apoptosis. Dysregulation of DSTYK has been linked to various cancers and other diseases, making it a target of interest for therapeutic strategies. Researchers are investigating the structural and functional characteristics of DSTYK to better understand its mechanism of action and the implications of its activity in human health. One pivotal aspect of this research involves the production of recombinant DSTYK proteins, which enable in-depth studies into the enzyme's kinetic properties, substrate interactions, and regulation. By utilizing recombinant DNA technology, scientists can express and purify DSTYK in various systems, facilitating the exploration of its role in cellular signaling networks. Overall, the comprehensive understanding of DSTYK's function and regulation may pave the way for novel therapeutic interventions in diseases associated with its dysregulation.
