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SF3a120 antibody - 204 011

SF3a 120 is a member of the U2 snRNP
Mouse monoclonal purified IgG
Cat. No.: 204 011
Amount: 100 µg
Price: $415.00
Cat. No. 204 011 100 µg purified IgG, lyophilized. For reconstitution add 100 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
Applications
 
WB: 1 : 1000 (AP staining) gallery  
IP: yes
ICC: 1 : 500 gallery  
IHC: yes
IHC-P: 1 : 500 gallery  

Western blot (WB); separation of proteins by PAGE and subsequent transfer to a membrane. Detection of target molecules is carried out with antibodies. Some antibodies require special sample preparation steps. For details, please refer to the “Remarks” section.

Immunoprecipitation (IP); Immunoisolation or pulldown of a target molecule using an antibody. For details and product specific hints, please refer to the ”Remarks” section.

Immunocytochemistry (ICC) on 4% PFA fixed cells. Immunoreactivity is usually revealed by fluorescence. Some antibodies require special fixation methods. For details, please refer to the “Remarks” section.

Immunohistochemistry (IHC) on 4% PFA perfusion fixed tissue with 24h PFA post fixation. Immunoreactivity is usually revealed by fluorescence or a chromogenic substrate. Some antibodies require special fixation methods or antigen retrieval steps. For details, please refer to the ”Remarks” section.

Immunohistochemistry (IHC-P) of formalin fixed, paraffin embedded (FFPE) tissue (some antibodies require special antigen retrieval steps, please refer to the ”Remarks” section). Immunoreactivity is usually revealed by fluorescence or a chromogenic substrate.

Clone 85D5
Subtype IgG1 (κ light chain)
Immunogen Recombinant protein corresponding to AA 1 to 793 from human SF3a120 (UniProt Id: Q15459)
Reactivity Reacts with: human (Q15459), rat (D3ZQM0), mouse (Q8K4Z5), mammals.
Other species not tested yet.
Data sheet 204_011.pdf

References for SF3a120 - 204 011

Isolation and characterization of post-splicing lariat-intron complexes.
Yoshimoto R, Kataoka N, Okawa K, Ohno M
Nucleic acids research (2009) 373: 891-902. 204 011 WB
Factors associated with a purine-rich exonic splicing enhancer sequence in Xenopus oocyte nucleus.
Masuyama K, Taniguchi I, Okawa K, Ohno M
Biochemical and biophysical research communications (2007) 3593: 580-5. 204 011 WB, IP
Factors associated with a purine-rich exonic splicing enhancer sequence in Xenopus oocyte nucleus.
Masuyama K, Taniguchi I, Okawa K, Ohno M
Biochemical and biophysical research communications (2007) 3593: 580-5. 204 011 WB, IP
In vivo 5-ethynyluridine (EU) labelling detects reduced transcription in Purkinje cell degeneration mouse mutants, but can itself induce neurodegeneration.
Van't Sant LJ, White JJ, Hoeijmakers JHJ, Vermeij WP, Jaarsma D
Acta neuropathologica communications (2021) 91: 94. 204 011 IHC; tested species: mouse
Cat. No.: 204 011
Amount: 100 µg
Price: $415.00
Isolation and characterization of post-splicing lariat-intron complexes.
Yoshimoto R, Kataoka N, Okawa K, Ohno M
Nucleic acids research (2009) 373: 891-902. 204 011 WB
Factors associated with a purine-rich exonic splicing enhancer sequence in Xenopus oocyte nucleus.
Masuyama K, Taniguchi I, Okawa K, Ohno M
Biochemical and biophysical research communications (2007) 3593: 580-5. 204 011 WB, IP
Factors associated with a purine-rich exonic splicing enhancer sequence in Xenopus oocyte nucleus.
Masuyama K, Taniguchi I, Okawa K, Ohno M
Biochemical and biophysical research communications (2007) 3593: 580-5. 204 011 WB, IP
In vivo 5-ethynyluridine (EU) labelling detects reduced transcription in Purkinje cell degeneration mouse mutants, but can itself induce neurodegeneration.
Van't Sant LJ, White JJ, Hoeijmakers JHJ, Vermeij WP, Jaarsma D
Acta neuropathologica communications (2021) 91: 94. 204 011 IHC; tested species: mouse
Background
In eukaryotic cells introns are removed from pre-mRNAs by the splicesome which consists of the U1, U2, U4, U5 and U6 small nuclear ribonucleoprotein particles (snRNPs) and other proteins.
The splicing factor SF3a is a member of the U2 snRNP. It is composed of three subunits (60 kDa, 66 kDa and 120 kDa) and has been shown to be essential for the assembly of functional 17S U2 snRNP in vitro.