Background:

The phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions in eukaryotes, including cell division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the serine/threonine (Ser/Thr) protein kinases. CLK1 (CDC-like kinase 1) and CLK4 (CDC-like kinase 4) are nuclear proteins that are members of the Ser/Thr protein kinase family. CLK1 and CLK4 catalyze the ATP-dependent phosphorylation of serine- and arginine-rich (SR) proteins within the spliceosomal complex and are thought to regulate the ability of SR proteins to control RNA splicing. Specifically, CLK1 may mediate the release of specific proteins from nuclear storage sites. Expression of CLK1 may be very low due to a premature stop codon in the mRNA, which leads to nonsense-mediated mRNA decay, while CLK4 is expressed in brain, liver, kidney, heart and muscle. CLK1 activity is positively regulated by phosphorylation on either tyrosine residues or serine/thre-onine residues. CLK1 activity is negatively regulated by steric constraints mediated by the N-terminal domain and also by phosphorylation on a subset of serine/threonine residues within the catalytic domain.

Alternative names:

CLK4; Dual specificity protein kinase CLK4; CDC-like kinase 4

Clonality:

Polyclonal

Reactivity:

Human,Mouse

Source:

Rabbit

Isotype:

Request info at info@sobekbio.com

Immunogen:

Synthesized peptide derived from the Internal region of human CLK4. at AA rangle； 70-150

Concentration:

1mg/ml

Applications:

Request info at info@sobekbio.com

Recommende dilutions:

Request info at info@sobekbio.com

Storage:

PBS with 0.02% sodium azide and 50% glycerol pH 7.4. Store at -20°C. Avoid repeated freeze-thaw cycles.

More info:

Email: info@sobekbio.com

Orders:

Email: orders@sobekbio.com