PSF Antibody [M17A24] Datasheet

Biological Description

Specificity	PSF Antibody [M17A24] detects endogenous levels of total PSF protein.
Background	PSF (Polypyrimidine tract-binding protein-associated splicing factor) belongs to the DBHS family of nuclear proteins and functions as a multifunctional nucleic acid-binding regulator of gene expression. The protein contains two RNA recognition motifs, a DNA-binding domain, and an N-terminal proline/glutamine-rich region that mediates protein-protein interactions. PSF represses transcription of multiple oncogenic genes through direct binding to their regulatory regions via its DNA-binding domain, while RNA-binding domains form complexes with non-coding VL30 retroelement RNA to release PSF repression and reverse transcriptional silencing. PSF stimulates splicing and 3'-end cleavage of pre-mRNA in a manner dependent on RNA polymerase II C-terminal domain phosphorylation and transcriptional activator strength, with distinct RNA recognition motifs playing nonredundant roles in promoting efficient cotranscriptional processing of 5'-proximal introns. PSF coordinates with p54nrb/NonO in spliceosomal complexes and interacts with U5 snRNP stem-loop 1 to recruit tri-snRNP subunits, ensuring accurate intron removal. The protein anchors hyper-edited RNAs in paraspeckles through high-affinity binding to inosine-rich sequences, preventing their cytoplasmic export until NEAT1 dissociation or specific cleavage relieves retention. PSF binds directly to double-strand breaks via its N-terminal RGG box through the proline-rich domain and recruits RAD51D recombinase for homologous recombination repair. Increased PSF expression inhibits proliferation and colony formation while suppressing oncogenes like P450ssc and GAGE6.

Specificity

PSF Antibody [M17A24] detects endogenous levels of total PSF protein.

Background

PSF (Polypyrimidine tract-binding protein-associated splicing factor) belongs to the DBHS family of nuclear proteins and functions as a multifunctional nucleic acid-binding regulator of gene expression. The protein contains two RNA recognition motifs, a DNA-binding domain, and an N-terminal proline/glutamine-rich region that mediates protein-protein interactions. PSF represses transcription of multiple oncogenic genes through direct binding to their regulatory regions via its DNA-binding domain, while RNA-binding domains form complexes with non-coding VL30 retroelement RNA to release PSF repression and reverse transcriptional silencing. PSF stimulates splicing and 3'-end cleavage of pre-mRNA in a manner dependent on RNA polymerase II C-terminal domain phosphorylation and transcriptional activator strength, with distinct RNA recognition motifs playing nonredundant roles in promoting efficient cotranscriptional processing of 5'-proximal introns. PSF coordinates with p54nrb/NonO in spliceosomal complexes and interacts with U5 snRNP stem-loop 1 to recruit tri-snRNP subunits, ensuring accurate intron removal. The protein anchors hyper-edited RNAs in paraspeckles through high-affinity binding to inosine-rich sequences, preventing their cytoplasmic export until NEAT1 dissociation or specific cleavage relieves retention. PSF binds directly to double-strand breaks via its N-terminal RGG box through the proline-rich domain and recruits RAD51D recombinase for homologous recombination repair. Increased PSF expression inhibits proliferation and colony formation while suppressing oncogenes like P450ssc and GAGE6.

Usage Information

Application

WB, IP, IHC, IF

Dilution

WB

1:500-1:1000

Reactivity

Human, Mouse

Source

Mouse Monoclonal Antibody

MW

80 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

References

https://pubmed.ncbi.nlm.nih.gov/16079199/
https://pubmed.ncbi.nlm.nih.gov/16024807/

Application Data

WB

Validated by Selleck

Lane 1: Hela, Lane 2: A431, Lane 3: HUVEC, Lane 4: HepG2