S4045
Monoclonal Anti-Splicing Factor SC-35 antibody produced in mouse
clone SC-35, ascites fluid
Synonym(s):
Anti-SC-35, Anti-SC35
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About This Item
Recommended Products
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
SC-35, monoclonal
mol wt
antigen 35 kDa (a doublet)
contains
15 mM sodium azide
species reactivity
frog, Drosophila, newt, rat, human
technique(s)
electron microscopy: suitable
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
indirect immunofluorescence: 1:2,000 using cultured human fibroblasts
isotype
IgG1
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... SFRS2(6427)
rat ... Sfrs2(494445)
General description
Monoclonal Anti-Splicing Factor SC-35 (mouse IgG1 isotype) is derived from the SC-35 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized RBF-DNJ mouse. Splicing component of 35 kDa (SC-35) is also termed as PR264. SC-35 displays a speckled distribution in the nucleus that co-localizes with small nuclear ribonucleoproteins (snRNPs), but unlike snRNPs, SC-35 does not give diffuse nuclear labeling.
Nuclear pre-mRNA splicing takes place in a multi-component structure termed a spliceosome. Major subunits of spliceosomes are U1, U2, U4/U6 and U5 small nuclear ribonucleoproteins (snRNP′s). In addition to the snRNP′s, a number of protein factors have been identified which are required for spliceosome assembly and splicing. For example, the protein factors U2AF, SF2 and SF3 are required for the binding of the U2 snRNP to the intron branch-point and for assembly of the pre-splicing complex. Two other non-snRNP splicing factors, SF2/ASF and SC-35 (splicing component of 35 kD, also termed PR264), are both required for the first step of splicing and spliceosome assembly. SF2/ASF and SC-35 are also involved in 5N splice site selection of alternatively spliced pre-mRNA′s.
The essential non-snRNP splicing factor SC-35 displays a speckled distribution in the nucleus that co-localizes with snRNPs, but unlike snRNPs, SC-35 does not give diffuse nuclear labelling. In the nucleus, snRNPs are concentrated in coiled bodies and in the speckled regions, whereas SC-35 is found in speckles but not in coiled bodies.
The essential non-snRNP splicing factor SC-35 displays a speckled distribution in the nucleus that co-localizes with snRNPs, but unlike snRNPs, SC-35 does not give diffuse nuclear labelling. In the nucleus, snRNPs are concentrated in coiled bodies and in the speckled regions, whereas SC-35 is found in speckles but not in coiled bodies.
Specificity
Recognizes a phospho-epitope on the non-snRNP (small nuclear ribonucleoprotein particles) factor SC-35. The antibody reacts with the splicing factor SC-35 and with the SC-35-related non-snRNP factor SF2/ASF. The antibody labels SC-35 as a speckled pattern in the nucleoplasm, excluding the nucleoli. Other uses include inhibition and depletion of splicing activity in nuclear extracts and immunoaffinity purification.
Immunogen
partially purified mammalian splicesome.
Application
Monoclonal Anti-Splicing Factor SC-35 antibody produced in mouse has been used in:
- fluorescence image analysis
- immunohistochemistry
- two or three color immunofluorescence staining
- enzyme-linked immunosorbent assay (ELISA)
- immunohistology
- immunoelectronmicroscopy
- immunoaffinity purification
- immunoprecipitation
Monoclonal Anti-Splicing Factor SC-35 may be used for the localization of SC-35 using ELISA, immunohistology and immunoelectronmicroscopy, for inhibition and depletion of splicing activity in nuclear extracts, and for immunoaffinity purification and immunoprecipitation.
Indirect immunofluorescence: a dilution of at least 1:2,000 was determined by staining cultured human fibroblasts.
Indirect immunofluorescence: a dilution of at least 1:2,000 was determined by staining cultured human fibroblasts.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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X D Fu et al.
Nature, 343(6257), 437-441 (1990-02-01)
A monoclonal antibody raised against mammalian spliceosomes specifically recognizes a non-snRNP factor required for spliceosome assembly. This splicing factor is highly concentrated in discrete regions within the nucleus, in a pattern that is a distinct subset of that seen with
Characterization and cloning of the human splicing factor 9G8: a novel 35 kDa factor of the serine/arginine protein family.
Cavaloc Y, et al.
The Embo Journal, 13(11), 2639-2649 (1994)
X D Fu et al.
Proceedings of the National Academy of Sciences of the United States of America, 89(23), 11224-11228 (1992-12-01)
The human pre-mRNA splicing factors SF2 and SC35 have similar electrophoretic mobilities, and both of them contain an N-terminal ribonucleoprotein (RNP)-type RNA-recognition motif and a C-terminal arginine/serine-rich domain. However, the two proteins are encoded by different genes and display only
D L Spector et al.
The EMBO journal, 10(11), 3467-3481 (1991-11-01)
SC-35 is a non-snRNP spliceosome component that is specifically recognized by the anti-spliceosome monoclonal antibody alpha SC-35. In this paper we provide direct evidence that SC-35 is an essential splicing factor and we examine the immunolocalization of SC-35 by confocal
Rad54B targeting to DNA double-strand break repair sites requires complex formation with S100A11
Murzik U, et al.
Molecular Biology of the Cell, 19(7), 2926-2935 (2008)
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