CLK3 Protein, Human (sf9, GST)

The CLK3 protein is a dual-specificity kinase that exerts catalytic activity on both serine/threonine and tyrosine-containing substrates. It plays a crucial role in phosphorylating serine- and arginine-rich (SR) proteins within the spliceosome complex, contributing to the complex network of regulatory mechanisms that control RNA splicing. CLK3 Protein, Human (sf9, GST) is the recombinant human-derived CLK3 protein, expressed by Sf9 insect cells , with N-GST labeled tag. The total length of CLK3 Protein, Human (sf9, GST) is 490 a.a., with molecular weight of ~70 kDa.

CLK3, a dual-specificity kinase, exhibits activity on both serine/threonine and tyrosine-containing substrates, particularly targeting serine- and arginine-rich (SR) proteins within the spliceosomal complex. This enzyme is integral to a regulatory network influencing the control of RNA splicing by SR proteins, leading to the redistribution of these proteins from speckles to a diffuse nucleoplasmic distribution. CLK3 specifically phosphorylates SRSF1 and SRSF3, key components of the splicing machinery. Moreover, it plays a role in the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells, suggesting its involvement in the intricate regulation of gene expression and splicing events within cellular processes.

Human

Sf9 insect cells

N-GST

P49761-1/NP_003983.2 (M1-R490)

1198  [NCBI]

Approximately 70 kDa

Greater than 80% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.