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P2860

Sigma-Aldrich

Monoclonal Anti-PSF antibody produced in mouse

clone B92, purified from hybridoma cell culture

Synonym(s):

Mouse Anti-Polypyrimidine tract-binding protein-associated splicing factor

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

B92, monoclonal

form

buffered aqueous solution

species reactivity

mouse, human

packaging

antibody small pack of 25 μL

concentration

~2 mg/mL

technique(s)

immunocytochemistry: suitable
immunohistochemistry (frozen sections): suitable
immunoprecipitation (IP): suitable
microarray: suitable
radioimmunoassay: suitable using cells
western blot: 2-4 μg/mL using whole extract of cultured HeLa cells

isotype

IgG1

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... TAP1(6890)

Related Categories

General description

Monoclonal Anti-PSF (mouse IgG1 isotype) is derived from the B92 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a C57BL/6J mouse immunized with a lysate of mouse bone marrow-derived stromal cell line. Polypyrimidine tract-binding protein-associated splicing factor (PSF) is an ubiquitous nuclear matrix protein. It is characterized with two consensus RNA-binding domains and an unusual amino terminus rich in proline and glutamine residues.

Immunogen

lysate of mouse bone marrow-derived stromal cell line.

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Immunohistochemistry (1 paper)
Immunoprecipitation (1 paper)
Monoclonal Anti-PSF antibody produced in mouse has been used in:
  • immunofluorescence
  • immunohistochemistry
  • immunoprecipitation

Biochem/physiol Actions

Polypyrimidine tract-binding protein-associated splicing factor (PSF) plays a pivotal role in mammalian spliceosome. PSF is also necessary for pre-mRNA splicing and transcription. The restricted expression of PSF suggests that it is involved in the control of neuronal-specific splicing events occurring at particular stages of neuronal differentiation and maturation. Monoclonal antibodies reacting specifically with PSF are useful tools for the molecular identification and characterization of the functional activity of PSF.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Preparation Note

Purified from culture supernatant of hybridoma cells grown in a bioreactor.

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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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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Human PSF concentrates DNA and stimulates duplex capture in DMC1-mediated homologous pairing.
Yuichi Morozumi, Ryohei Ino
Nucleic Acids Research, 40(7), doi: 10-doi: 10 (2011)
Feng Chi et al.
PloS one, 7(4), e35862-e35862 (2012-04-27)
IbeA-induced NF-κB signaling through its primary receptor vimentin as well as its co-receptor PSF is required for meningitic E. coli K1 penetration and leukocyte transmigration across the blood-brain barrier (BBB), which are the hallmarks of bacterial meningitis. However, it is
Guillaume Cornelis et al.
RNA biology, 13(9), 826-836 (2016-06-18)
Long non-coding RNAs (lncRNAs) are widely expressed and play various roles in cell homeostasis. However, because of their low conservation at the sequence level, recapitulating lncRNA evolutionary history is often challenging. While performing an ultrastructural analysis of viral particles present
Cytoplasmic Relocalization of TAR DNA-Binding Protein 43 Is Not Sufficient to Reproduce Cellular Pathologies Associated with ALS In vitro
Wobst HJ, et al.
Frontiers in Molecular Neuroscience, 10(7) (2017)
Differential nuclear localization and nuclear matrix association of the splicing factors PSF and PTB
Meissner M, et al.
Journal of Cellular Biochemistry, 76(4), 559-566 (2000)

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