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SAB4200725

Sigma-Aldrich

Anti-Splicing Factor SC-35 antibody, Mouse monoclonal

clone SC-35, purified from hybridoma cell culture

Synonyme(s) :

Anti-PR264, Anti-SFRS2, Anti-SFRS2A, Anti-SRp30b, Anti-Splicing component 35 kDa (SC35), Anti-serine/arginine-rich splicing factor 2 (SRSF2)

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.43

Source biologique

mouse

Forme d'anticorps

purified from hybridoma cell culture

Type de produit anticorps

primary antibodies

Clone

SC-35, monoclonal

Forme

buffered aqueous solution

Poids mol.

~35 kDa

Espèces réactives

human, mouse, quail, hamster, frog, porcine, rat

Concentration

~1.0 mg/mL

Technique(s)

ELISA: suitable
dot blot: suitable
immunoblotting: suitable
immunofluorescence: 0.125-0.25 μg/mL using HeLa cells
immunohistochemistry: suitable
immunoprecipitation (IP): suitable

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... SRSF2(6427)

Description générale

Anti-Splicing Factor SC-35 antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the SC-35 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a RBF-DHJ mouse immunized with partially purified spliceosomes prepared from HeLa cells. Splicing Factor SC-35, also known as serine/arginine rich splicing factor 2 (SRSF2) belongs to the family of of serine/arginine-rich (SR) proteins.

Immunogène

partially purified spliceosomes prepared from HeLa cells

Application

Anti-Splicing Factor SC-35 antibody has been used in
  • dot blot
  • enzyme linked immunosorbent assay (ELISA)
  • immunofluorescence
  • immunohistochemistry
  • immunoblotting
  • immunoprecipitation

Actions biochimiques/physiologiques

Splicing Factor SC-35 are critical regulators of constitutive and alternative pre-mRNA splicing. It also controls cellular apoptosis in response to genotoxic stress. Serine/arginine protein kinase 1 (SRPK1) specifically phosphorylates SC-35, resulting in p53 suppression and cyclin D1 upregulation. Elevated levels of SC-35 correlate with aggressive phenotype in several cancer types including lung squamous cell carcinoma and lung adenocarcinoma. SC-35 has oncogenic function in tumor progression of human papilloma virus (HPV)-infected cells.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Valerie Edmond et al.
The EMBO journal, 30(3), 510-523 (2010-12-16)
SRSF2 is a serine/arginine-rich protein belonging to the family of SR proteins that are crucial regulators of constitutive and alternative pre-mRNA splicing. Although it is well known that phosphorylation inside RS domain controls activity of SR proteins, other post-translational modifications
E2F1 controls alternative splicing pattern of genes involved in apoptosis through upregulation of the splicing factor SC35
Merdzhanova L, et al.
Cell Death and Differentiation, 15(12), 1815-1815 (2008)
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
M Carmo-Fonseca et al.
The EMBO journal, 10(7), 1863-1873 (1991-07-01)
The in vivo distribution of snRNPs has been analysed by microinjecting fluorochrome-labelled antisense probes into the nuclei of live HeLa and 3T3 cells. Probes for U2 and U5 snRNAs specifically label the same discrete nuclear foci while a probe for
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

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