Recombinant Mouse Death-associated protein kinase 1 (Dapk1), partial

Code CSB-YP006499MO
MSDS
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Source Yeast
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Code CSB-EP006499MO
MSDS
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Source E.coli
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Code CSB-EP006499MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP006499MO
MSDS
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Source Baculovirus
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Code CSB-MP006499MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Dapk1
Uniprot No.
Alternative Names
Dapk1Death-associated protein kinase 1; DAP kinase 1; EC 2.7.11.1
Species
Mus musculus (Mouse)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3. Acts as a signaling amplifier of NMDA receptors at extrasynaptic sites for mediating brain damage in stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex and it phosphorylates GRINB at Ser-1303 inducing injurious Ca(2+) influx through NMDA receptor channels, resulting in an irreversible neuronal death. Required together with DAPK3 for phosphorylation of RPL13A upon interferon-gamma activation which is causing RPL13A involvement in transcript-selective translation inhibition.
Gene References into Functions
  1. DAPK deficiency leads to excess HIF-1a accumulation, enhanced IL-17 expression and exacerbated experimental autoimmune encephalomyelitis. PMID: 27312851
  2. Excitotoxicity can proceed without increased Ser-1303 phosphorylation, and is unaffected by Dapk1 deficiency in vitro or following ischemia in vivo. PMID: 28731405
  3. Authors find that the LTP specificity of CaMKII synaptic accumulation is due to its LTD-specific suppression by calcineurin (CaN)-dependent DAPK1 activation, which in turn blocks CaMKII binding to GluN2B. PMID: 28614711
  4. DAPK1 specifically phosphorylates NDRG2 Ser350 and this phosphorylation is an important caspase-dependent mechanism by which NDRG2 mediates cell death in neuronal cells. PMID: 28141794
  5. Inhibition of DAPK1 by deleting a catalytic domain or a death domain of DAPK1 rescues the Excitatory pyramidal neurons in the entorhinal cortical layer II region synaptic loss PMID: 27798139
  6. in Alzheimer's disease (AD) brains, elevated DAPK1 levels showed co-relation with the increase of APP phosphorylation. Combined together, these results suggest that DAPK1 promotes the phosphorylation and amyloidogenic processing of APP, and that may serve a potential therapeutic target for AD. PMID: 27094130
  7. This study demonstrate that phosphorylation of Tau at Serine 262 by the kinase domain of DAPK1 mediates spine damage and the subsequent neuronal death in ischemic stroke. PMID: 25995053
  8. DAPK1-p53 interaction is a preferred target for therapeutic intervention of stroke. PMID: 25139875
  9. Suggest that DAPK1 is a novel regulator of tau protein abundance, and that DAPK1 upregulation might contribute to tau-related pathologies in Alzheimer disease. PMID: 24853415
  10. the DAPK1-p53 interaction is a signaling point of convergence of necrotic and apoptotic pathways PMID: 24806680
  11. TSC2 binds to the death domain of DAPK. This interaction is required for TSC2 to reduce DAPK protein levels and half-life. DAPK is regulated by the lysosome pathway. Lysosome inhibition blocks TSC2-mediated degradation of DAPK. PMID: 21134130
  12. Results identify DAPK as a molecule required for full production of IL-1beta and functional assembly of the NLRP3 inflammasome. PMID: 21041719
  13. Study reports that cerebral ischemia recruits death-associated protein kinase 1 (DAPK1) into the NMDA receptor NR2B protein complex in the cortex of adult mice. PMID: 20141836
  14. Death-associated protein kinase (DAPK) is regulated by DANGER which binds directly to DAPK and inhibits catalytic activity. PMID: 20053891
  15. cellular activities of DAPK are critical for antagonizing caspase-dependent apoptosis to promote cell survival under normal cell growth conditions. PMID: 14530257
  16. DAPK has a role in tubular cell apoptosis and renal dysfunction after IR injury PMID: 15213270
  17. kinase domain of Dapk1 deleted by gene targeting plays a suppressive role for the development of renal fibrosis through inhibition of the tubular epithelial-to-mesenchymal transition in a mouse model of chronic obstructive uropathy PMID: 15583830
  18. Results revealed crucial implications of DAPK in regulating spatial memory. PMID: 16596273
  19. show a critical role for C/EBP-beta in a novel IFN-induced cell growth-suppressive pathway via DAPK1 PMID: 18250155
  20. DAPk constitutes a critical integration point in endoplasmic reticulum stress signaling. PMID: 18806755
  21. a novel interaction between DAPK and TSC2 proteins that has revealed a positive link between growth factor stimulation of DAPK and mTORC1 signaling that may ultimately affect autophagy, cell survival, or apoptosis. PMID: 18974095
  22. DAPK positively regulates intracellular signaling pathways for CPT-11-induced granulosa cell apoptosis PMID: 19287947

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Protein Families
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily
Tissue Specificity
High levels in bladder, uterus, vas deferens, lung, liver and kidney.
Database Links
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