R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
SRSF3 (E9U9C) Rabbit mAb #35073
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 20, 22 |
| Source/Isotype | Rabbit IgG |
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
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
SRSF3 (E9U9C) Rabbit mAb recognizes endogenous levels of total SRSF3 protein.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Asn89 of human SRSF3 protein.
Background
Serine/arginine-rich splicing factor 3 (SRSF3), also known as SRP20, is a member of the highly conserved family of SR proteins responsible for splicing regulation (1,2). SRSF3 promotes exon inclusion by enhancing the recognition of weak splice acceptor sites, a function that also regulates its own mRNA by including exon 4. This function is antagonized by another SR family member, SRSF1 (3). SRSF3 can be shuttled in and out of the cytoplasm, where it plays a role in mRNA export along with SRSF7 (3,4). SRSF3 and SRSF7 have been shown to exert opposing effects on 3’UTR length by recruiting various proteins upstream of polyadenylation sites (5,6). SRSF3 has been shown to be regulated by an epitranscriptomic mechanism, as the m6a-binding factor YTHDC1 recruits SRSF3 to promote exon inclusion, while blocking the binding of SRSF10 (7). SRSF3 has been identified as an oncogene, which through its autoregulation and alternative splicing of other proteins, can drive many different cancer types (8-12).
- Jumaa, H. et al. (1997) Mol Cell Biol 17, 3116-24.
- Blencowe, B.J. et al. (1999) Biochem Cell Biol 77, 277-91.
- Jumaa, H. and Nielsen, P.J. (1997) EMBO J 16, 5077-85.
- Cáceres, J.F. et al. (1998) Genes Dev 12, 55-66.
- Lou, H. et al. (1998) Mol Cell Biol 18, 4977-85.
- Schwich, O.D. et al. (2021) Genome Biol 22, 82.
- Xiao, W. et al. (2016) Mol Cell 61, 507-519.
- Stickeler, E. et al. (1999) Oncogene 18, 3574-82.
- He, X. et al. (2011) Oncogene 30, 356-65.
- Kano, S. et al. (2014) Am J Physiol Cell Physiol 306, C250-62.
- Gautrey, H. et al. (2015) RNA Biol 12, 1139-51.
- Peiqi, L. et al. (2016) Int J Med Sci 13, 533-9.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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