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Merck
모든 사진(1)

주요 문서

SAB4200725

Sigma-Aldrich

Anti-Splicing Factor SC-35 antibody, Mouse monoclonal

clone SC-35, purified from hybridoma cell culture

동의어(들):

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

UNSPSC 코드:
12352203
NACRES:
NA.43

생물학적 소스

mouse

항체 형태

purified from hybridoma cell culture

항체 생산 유형

primary antibodies

클론

SC-35, monoclonal

양식

buffered aqueous solution

분자량

~35 kDa

종 반응성

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

농도

~1.0 mg/mL

기술

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

UniProt 수납 번호

배송 상태

dry ice

저장 온도

−20°C

타겟 번역 후 변형

unmodified

유전자 정보

human ... SRSF2(6427)

일반 설명

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.

면역원

partially purified spliceosomes prepared from HeLa cells

애플리케이션

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

생화학적/생리학적 작용

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.

물리적 형태

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

면책조항

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 Code

10 - Combustible liquids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable


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문서 라이브러리 방문

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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