
Thermo Fisher Scientific SR Monoclonal Antibody (16H3 (16H3E8))
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Applications
Tested Dilution
Publications
Western Blot (WB)
3-5 µg/mL
View 12 publications 12 publications
Immunocytochemistry (ICC/IF)
0.5-2 µg/mL
View 2 publications 2 publications
ELISA (ELISA)
0.1-1 µg/mL
Immunoprecipitation (IP)
-
View 2 publications 2 publications
Miscellaneous PubMed (Misc)
-
View 3 publications 3 publications
Product Specifications
Species Reactivity
Bovine, Dog, Chicken, Fruit fly, Human, Mouse, Rabbit, Rat, Xenopus
Published species
Human, Mouse, Rat
Host/Isotype
Mouse / IgG1, kappa
Class
Monoclonal
Type
Antibody
Clone
16H3 (16H3E8)
Immunogen
Purified, de-phosphorylated bovine Srp55 and Drosophila p55-GST. The 16H3 epitope has been mapped to a 40-amino acid polypeptide composed almost exclusively of arginine alternating with glutamate and aspartate
Conjugate
Unconjugated Unconjugated Unconjugated
Form
Liquid
Concentration
0.5 mg/mL
Purification
Protein A
Storage buffer
PBS, pH 7.4
Contains
0.1% sodium azide
Storage conditions
Maintain refrigerated at 2-8°C for up to 1 month. For long term storage store at -20°C
Shipping conditions
Ambient (domestic); Wet ice (international)
RRID
AB_2533149
Product Specific Information
This monoclonal antibody can be used to detect a sub-set of the non-snRNP splicing factors termed SR proteins. The antibody detects SRp75, SRp55, SRp40, and SRp20 but not SRp30a or b (ASF/SF2, SC-35) proteins. 16H3 also recognizes approximately 20 distinct nuclear proteins including the U1 70K component of the U1 snRNP and both subunits of U2AF. The epitope detected by the 16H3 monoclonal antibody has been termed the ″alternating arginine domain″ and is composed almost exclusively of argnine alternating with glutamate and aspartate. 16H3 targets are predominantly nuclear, nonnucleolar, and are localized to active sites of polymerase II transcription.
Target Information
SR proteins are a highly conserved family of arginine/serine-rich, spliceosome-associated phosphoproteins essential for metazoan pre-mRNA splicing. SR proteins act early in splicing by promoting splice site recognition and spliceosome assembly. SR proteins also play a regulatory role because they can determine alternative splice site usage in vivo and in vitro. SR proteins appear to be recruited from nuclear ″speckles″, in which they are concentrated to sites of transcription in order to spatially coordinate transcription and pre-mRNA splicing within the cell nucleus.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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