Analytical Data
-
Gene name
DAPK2
- Application
-
Alternative Names
DAPK2；Death-associated Protein kinase 2
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UIK4
-
Expression Region
1-370aa
-
AA Sequence
MFQASMRSPN MEPFKQQKVE DFYDIGEELG SGQFAIVKKC REKSTGLEYA AKFIKKRQSR ASRRGVSREE IEREVSILRQ VLHHNVITLH DVYENRTDVV LILELVSGGE LFDFLAQKES LSEEEATSFI KQILDGVNYL HTKKIAHFDL KPENIMLLDK NIPIPHIKLI DFGLAHEIED GVEFKNIFGT PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANIT AVSYDFDEEF FSQTSELAKD FIRKLLVKET RKRLTIQEAL RHPWITPVDN QQAMVRRESV VNLENFRKQY VRRRWKLSFS IVSLCNHLTR SLMKKVHLRP DEDLRNCESD TEEDIARRKA LHPRRRSSTS
-
Molecular Weight
42.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
DAPK2 (Death-associated protein kinase 2) is a serine/threonine kinase that plays a crucial role in various cellular processes, including apoptosis, autophagy, and cell differentiation. Its involvement in these pathways has made it a significant focus of research, particularly in the context of cancer and neurodegenerative diseases. DAPK2 is activated by stress signals and is known to interact with several key proteins that mediate cell death and survival. Given its functional importance, understanding the molecular mechanisms of DAPK2 is vital for identifying potential therapeutic targets. The development of recombinant DAPK2 protein is essential for detailed biochemical and structural studies, allowing researchers to investigate its enzymatic activity, binding interactions, and regulatory mechanisms. Furthermore, recombinant DAPK2 can be utilized in cellular assays to explore its role in disease models and to screen for small molecules that modulate its activity. By unraveling the complexities of DAPK2 function, researchers aim to enhance our understanding of its contributions to pathophysiological conditions and to develop innovative strategies for treatment.
