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Human CALML3 Protein (His Tag)

CLP

Catalog Number P12480-H07E
Organism Species Human
Host E. coli
Synonyms CLP
Molecular Weight The recombinant human CALML3 consisting of 164 amino acids and has a calculated molecular mass of 18.7KDa. It migrates as an 16 kDa band in SDS-PAGE under reducing conditions.
predicted N Met
SDS-PAGE
Purity > 95 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human CALML3 (P27482) (Met 1-Lys 149) was expressed, with a polyhistide tag at the N-terminus.
Bio-activity
Research Area Neuroscience |Neurotransmission |Calcium Signaling |Calmodulin Pathway
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Calmodulin-like protein 3 (CALML3) is similar to that of authentic calmodulin and may actually compete with calmodulin by binding, with different affinity, to cellular substrates. Calmodulin-like protein 3 (CALML3) is a tumor-sensitive protein specifically expressed in normal epithelial cells but downregulated in tumorigenesis. Downregulation of the protein is an early event in breast cancer development. One of the most pressing questions raised by the discovery of CLP/CALML3 is that of its potential targets. Although it is 85% identical to human calmodulin, the distinct properties of CLP suggest that it has specific targets or targets that only partially overlap with those of calmodulin. Research has identified the unconventional myosin-10 (Myo10) as a specific target of CALML3. The discovery of Myo10 as a specific target of CALML3 is highly significant and suggests multiple lines of further research such as investigations of the Ca2+ regulation of Myo10 and the role of the loss of CLP in epithelial differentiation, adhesion, and cancer. Cells expressing CALML3 displayed a striking increase in the number and length of myosin-10-positive filopodia and showed increased mobility in a wound healing assay.
Reference
  • Bennett RD, et al. (2007) Calmodulin-like protein increases filopodia-dependent cell motility via up-regulation of myosin-10. J Biol Chem. 282(5): 3205-12.
  • Perochon A, et al. (2011) Calmodulin and calmodulin-like proteins in plant calcium signaling. Biochimie. 93(12): 2048-53.
  • Chinpongpanich A, et al. (2011) Biophysical characterization of calmodulin and calmodulin-like proteins from rice, Oryza sativa L. Acta Biochim Biophys Sin (Shanghai). 43(11): 867-76.