Analytical Data
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Gene name
DAPK3
- Application
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Alternative Names
DAPK3；ZIPK；Death-associated Protein kinase 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
O43293
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Expression Region
1-454aa
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AA Sequence
MSTFRQEDVE DHYEMGEELG SGQFAIVRKC RQKGTGKEYA AKFIKKRRLS SSRRGVSREE IEREVNILRE IRHPNIITLH DIFENKTDVV LILELVSGGE LFDFLAEKES LTEDEATQFL KQILDGVHYL HSKRIAHFDL KPENIMLLDK NVPNPRIKLI DFGIAHKIEA GNEFKNIFGT PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGE TKQETLTNIS AVNYDFDEEY FSNTSELAKD FIRRLLVKDP KRRMTIAQSL EHSWIKAIRR RNVRGEDSGR KPERRRLKTT RLKEYTIKSH SSLPPNNSYA DFERFSKVLE EAAAAEEGLR ELQRSRRLCH EDVEALAAIY EEKEAWYREE SDSLGQDLRR LRQELLKTEA LKRQAQEEAK GALLGTSGLK RRFSRLENRY EALAKQVASE MRFVQDLVRA LEQEKLQGVE CGLR
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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
DAPK3 (Death Associated Protein Kinase 3) is a serine/threonine kinase that plays a crucial role in various cellular processes, including apoptosis, autophagy, and cellular signaling pathways. Emerging research indicates that DAPK3 can act as a tumor suppressor and is implicated in several cancer types, where its activity may regulate cell death and survival. Its reorganization into functional protein forms is essential for delving into its biochemical properties and understanding its role in disease mechanisms. Furthermore, the therapeutic potential of targeting DAPK3 pathways has garnered interest, as modulation of its activity could offer novel strategies for cancer treatment. The study of DAPK3, therefore, encompasses a multidisciplinary approach, integrating molecular biology, biochemistry, and pharmacology to elucidate its functions and develop potential therapeutic interventions. As a result, the production and characterization of recombinant DAPK3 protein are fundamental for advancing our understanding of its structure-function relationships and for the development of specific inhibitors or modulators that can influence its activity in pathological conditions. This research avenue holds promise for addressing gaps in our current knowledge and for paving the way toward innovative therapeutic strategies in oncology and possibly other related fields.
