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Merck

SAB4200501

Sigma-Aldrich

Anti-SFPQ antibody, Mouse monoclonal

clone FC23, purified from hybridoma cell culture

Sinónimos:

Monoclonal Anti-SFPQ antibody produced in mouse

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

FC23, monoclonal

form

buffered aqueous solution

mol wt

antigen ~95 kDa

species reactivity

rat, human, mouse

concentration

~1.0 mg/mL

technique(s)

indirect immunofluorescence: 10-20 μg/mL using HeLa cells.
western blot: 0.5-1 μg/mL using Whole extracts of mouse Hepa1-6 cells.

isotype

IgG2a

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SFPQ(6421)
mouse ... Sfpq(71514)
rat ... Sfpq(252855)

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General description

Splicing factor proline and glutamine rich (SFPQ), also known as polypyrimidine tract-binding protein-associated-splicing factor (PSF), is a multifunctional nuclear protein. It is encoded by the gene mapped to human chromosome 1p34. The encoded protein is characterized with an N-terminal glycine rich domain, a proline/glutamine-rich domain (P/Q), two RNA recognition motifs (RRMs) and a C-terminal region with two nuclear localization signals.
Splicing factor, praline- and glutamine-rich (SFPQ), also known as PSF, is a member of the DBHS (Drosophila behaviour, human splicing) protein family, consisting also of PSPC1 (paraspeckle protein 1) and NONO (non-POU-domain-containing, octamer binding protein). The DBHS proteins localizes between the nucleoplasm, paraspeckles and the nucleolus. Monoclonal Anti-SFPQ (mouse IgG2a isotype) is derived from the hybridoma FC23 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to a sequence at the C-terminal region of mouse SFPQ, conjugated to keyhole limpet hemocyanin (KLH).

Immunogen

Synthetic peptide corresponding to a sequence at the C-terminal region of mouse SFPQ, conjugated to KLH. The corresponding sequence is identical in rat and human.

Application

Monoclonal Anti-SFPQ antibody produced in mouse has been used in immunoblotting and immunofluorescence.

Biochem/physiol Actions

Drosophila behaviour, human splicing (DBHS) proteins are involved in several biological processes such as regulation of circadian rhythm, carcinogenesis and cancer progression. SFPQ activates androgen receptor mediated transcription.
Splicing factor proline and glutamine rich (SFPQ) along with its binding partner non-POU domain-containing octamer-binding protein (NONO/p54nrb), plays a vital role in RNA processing, RNA splicing and transcriptional regulation. Additionally, these proteins also play a crucial role in various regulatory roles including, selective nuclear retention of defective mRNAs. SFPQ participates in transcription repression by recruiting transcription regulator proteins Sin3a and histone deacetylase (HDAC).

Physical form

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

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

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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The t(1;9)(p34;q34) and t(8;12)(p11;q15) fuse pre-mRNA processing proteins SFPQ (PSF) and CPSF6 to ABL and FGFR1.
Hidalgo-Curtis C
Genes Chromosomes Cancer, 47, 379-385 (2008)
Arginine methylation and citrullination of splicing factor proline- and glutamine-rich (SFPQ/PSF) regulates its association with mRNA
Snijders AP
RNA, 21, 347-359 (2015)
PSPC1, NONO, and SFPQ are expressed in mouse Sertoli cells and may function as coregulators of androgen receptor-mediated transcription
Kuwahara S, et al.
Biology of Reproduction, 75(3), 352-359 (2006)
Paraspeckles: nuclear bodies built on long noncoding RNA
Bond S and Fox AH
The Journal of Cell Biology, 186(5), 637-644 (2009)
Structure of the heterodimer of human NONO and paraspeckle protein component 1 and analysis of its role in subnuclear body formation
Passon DM, et al.
Proceedings of the National Academy of Sciences of the USA, 109(13), 4846-4850 (2012)

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