SR Proteins (Non-snRNP Splicing Factor) (APC)

Cat# S6570-APC-100ul

Size : 100ul

Marca : US Biological

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S6570-APC SR Proteins (Non-snRNP Splicing Factor) (APC)

Clone Type
Polyclonal
Host
mouse
Isotype
IgG1,k
Grade
Affinity Purified
Applications
FLISA IC IF WB
Crossreactivity
Ca Ch Hu Mo Rb Rt Xe
Shipping Temp
Blue Ice
Storage Temp
4°C Do Not Freeze

SR proteins are a highly conserved family of arginine/serine rich, spliceosome associated phosphoproteins essential for metazoan pre-mRNA splicing. SR proteins appear to 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-a particularly interesting example is the regulation of adenovirus alternative RNA splicing by dephosphorylation of SR proteins. 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. ||The epitope detected by the antibody has been termed the “alternating arginine domain” and is composed almost exclusively of argnine alternating with glutamate and aspartate. Antibody targets are predominantly nuclear, nonnucleolar, and are localized to active sites of polymerase II transcription. Epitope is conserved in metazoans.||Applications: |Suitable for use in Immunofluorescence, Immunocytochemistry, FLISA and Western Blot. Other applications not tested.||Recommended Dilutions:|Optimal dilutions to be determined by the researcher.||Positive Controls: |HeLa cell, nuclear extracts||Storage and Stability:|Store product at 4°C in the dark. DO NOT FREEZE! Stable at 4°C for 12 months after receipt as an undiluted liquid. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. Caution: APC conjugates are sensitive to light. For maximum recovery of product, centrifuge the original vial prior to removing the cap. ||Note: Applications are based on unconjugated antibody.

Applications
Product Type: Mab|Isotype: IgG1,k|Clone No: 3G269|Host: mouse|Concentration: As Reported|Form: Supplied as a liquid in PBS, pH 7.2. Labeled with Allophycocyanin (APC).|Purity: Purified by Protein A affinity chromatography|Immunogen: Purified, de-phosphorylated bovine Srp55 and Drosophila p55-GST. The epitope has been mapped to a 40 amino acid polypeptide composed almost exclusively of arginine alternating with glutamate and aspartate.|Specificity: Recognizes a sub-set of the non-snRNP splicing factors termed SR proteins. Detects SRp75, SRp55, SRp40 and SRp20 but not SRp30a or b (ASF/SF2, SC-35) proteins. Recognizes ~20 distinct nuclear proteins including the U1 70K component of the U1 snRNP and both subunits of U2AF1. Species Crossreactivity: chicken, human, mouse, rabbit, canine, rat, Xenopus. Reactivity has not been detected with yeasts. ||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Immunogen
Purified, de-phosphorylated bovine Srp55 and Drosophila p55-GST. The epitope has been mapped to a 40 amino acid polypeptide composed almost exclusively of arginine alternating with glutamate and aspartate.
Form
Supplied as a liquid in PBS, pH 7.2. Labeled with Allophycocyanin (APC).
Purity
Purified by Protein A affinity chromatography
Specificity
Recognizes a sub-set of the non-snRNP splicing factors termed SR proteins. Detects SRp75, SRp55, SRp40 and SRp20 but not SRp30a or b (ASF/SF2, SC-35) proteins. Recognizes ~20 distinct nuclear proteins including the U1 70K component of the U1 snRNP and both subunits of U2AF1. Species Crossreactivity: chicken, human, mouse, rabbit, canine, rat, Xenopus. Reactivity has not been detected with yeasts.
References
1. Neugebauer, KM, et al., J Cell Biol 129:899–908 (1995). 2. Tacke R and Manley JL, Proc Soc Exp Biol Med 220:59–63 (1999). 3. Graveley BR et al., Curr Biol 9:R6–7 (1999). 4. Fu X-D, Nature 365:82–85 (1993). 5. Zahler AM et al., Science 260:219–222 (1993). 6. Caceres JF, Science 265:1706–1709 (1994). 7. Kanopka A et al., Nature 393:185–7 (1998). 8. Misteli T et al., Nature 387:523–527 (1997).