Analytical Data
-
Gene name
VRK3
- Application
-
Alternative Names
VRK3；Serine/threonine-Protein kinase VRK3
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8IV63
-
Expression Region
1-474aa
-
AA Sequence
MISFCPDCGKSIQAAFKFCPYCGNSLPVEEHVGSQTFVNPHVSSFQGSKR GLNSSFETSPKKVKWSSTVTSPRLSLFSDGDSSESEDTLSSSERSKGSGS RPPTPKSSPQKTRKSPQVTRGSPQKTSCSPQKTRQSPQTLKRSRVTTSLE ALPTGTVLTDKSGRQWKLKSFQTRDNQGILYEAAPTSTLTCDSGPQKQKF SLKLDAKDGRLFNEQNFFQRAAKPLQVNKWKKLYSTPLLAIPTCMGFGVH QDKYRFLVLPSLGRSLQSALDVSPKHVLSERSVLQVACRLLDALEFLHEN EYVHGNVTAENIFVDPEDQSQVTLAGYGFAFRYCPSGKHVAYVEGSRSPH EGDLEFISMDLHKGCGPSRRSDLQSLGYCMLKWLYGFLPWTNCLPNTEDI MKQKQKFVDKPGPFVGPCGHWIRPSETLQKYLKVVMALTYEEKPPYAMLR NNLEALLQDLRVSPYDPIGLPMVP
-
Molecular Weight
80 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
The study of VRK3 (Vaccinia-related kinase 3) recombinant protein has gained significant attention in recent years due to its potential roles in cellular processes and disease mechanisms. VRK3 is part of the VRK family of serine/threonine kinases, which are implicated in various cellular functions, including cell cycle regulation, DNA damage response, and apoptosis. Research has shown that VRK3 is involved in the phosphorylation of key substrates that contribute to the regulation of gene expression and cell proliferation. Additionally, alterations in VRK3 expression or activity have been associated with several pathological conditions, including cancer, making it a compelling target for therapeutic intervention. Understanding the structure and function of VRK3 recombinants can provide insight into the molecular pathways involved in these diseases. Furthermore, utilizing recombinant techniques allows for the production of purified VRK3 proteins, enabling detailed biochemical and biophysical studies. These investigations could lead to the identification of novel drug targets and the development of innovative therapeutic strategies, positioning VRK3 as a significant focus in the field of biomedical research. As the exploration of VRK3 progresses, its role in health and disease may become more defined, paving the way for future applications in clinical settings.
