Phospho-SRPK2 (Ser497) Antibody #23708
- WB
- IP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 115 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Phospho-SRPK2 (Ser497) Antibody recognizes endogenous levels of SRPK2 protein only when phosphorylated at Ser497. The antibody is specific to SRPK2 (Ser497) due to the absence of an equivalent phosphorylation site in both SPRK1 and SPRK3.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser497 of human SRPK2 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Serine/arginine-rich protein-specific kinases (SRPKs) are a small family of serine/threonine protein kinases that phosphorylates serine residues in sequence regions containing repetitive serine/arginine-rich dipeptides (SR domains). There are three known family members (SRPK1-3), of which SRPK1 and SRPK2 are the most well-studied. Multiple research studies have shown these kinases play an important role in post-transcriptional regulation, notably via phosphorylation of SR-family RNA splicing factors (1). SRPK2 has also been implicated in lipid biogenesis, following activation through sequential phosphorylation by mTORC-activated S6K1 and casein kinase 1 (2). Phosphorylation of SRPK2 at Ser494 and Ser497 promotes nuclear translocation of SRPK2, thereby enabling its regulation of mRNA splicing factors involved in lipid biogenesis. Notably, SRPK1 and SRPK2 have both been implicated in the phosphorylation of key viral proteins (3), including the nucleocapsid protein of the SARS and SARS-CoV-2 coronaviruses (4), a modification that may be essential for viral replication.
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