Description
Recombinant Mouse CAMK4/CaMKIV Protein (Active) | PKSM040459 | Gentaur US, UK & Europe Disrtribition
Synonyms: A430110E23Rik;AI666733;CaMKIV;CaMKIV/Gr;D18Bwg0362e
Active Protein: N/A
Activity: A DNA sequence encoding the mouse CAMK4(P08414) (Met1-Tyr469) was expressed and purified with two additional amino acids (Gly & Pro ) at the N-terminus.
Protein Construction: A DNA sequence encoding the mouse CAMK4(P08414) (Met1-Tyr469) was expressed and purified with two additional amino acids (Gly & Pro ) at the N-terminus.
Fusion Tag: N/A
Species: Mouse
Expressed Host: Baculovirus-Insect Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 52.7 kDa
Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, 10% glycerol, pH 7.4
Reconstitution: Please refer to the printed manual for detailed information.
Background: Ca2+/ calmodulin-dependent protein kinase 4 (CAMKⅣ) belongs to the serine/threonine protein kinase family, and to the Ca2+/calmodulin-dependent protein kinase subfamily which is widely recognized as an essential enzyme implicated in the phophoinositide amplification cascade. Ca2+/calmodulin dependent protein kinase (CAMK) can be activated by the introcellular increased Ca2+ and then apt to combine with the target protein. Ca2+/ calmodulin-dependent protein kinase 4 (CAMKⅣ) is a multifunctional CaM-dependent kinase protein with limited tissue distribution, that has been implicated in transcriptional regulation in lymphocytes, neurons and male germ cells. All of the isforms of this family, including myosin light chain kinase, phosphorylase kinase, CaMK1, CaMKⅢ and CaMKⅣ have EF-hand structure.
Research Area: N/A
