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Merck
CN

SAB4200188

Sigma-Aldrich

Anti-U1 snRNP C (U1C) antibody, Rat monoclonal

clone 4H12, purified from hybridoma cell culture

别名:

Anti-Snrp1c, Anti-Snrpc, Anti-U1 small nuclear ribonucleoprotein C, Anti-U1-C, Anti-U1C

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About This Item

UNSPSC代码:
12352203
NACRES:
NA.41

生物来源

rat

偶联物

unconjugated

抗体形式

purified from hybridoma cell culture

抗体产品类型

primary antibodies

克隆

4H12, monoclonal

表单

buffered aqueous solution

分子量

~20 kDa

种属反应性

human, mouse, rat, hamster, monkey

浓度

~1.0 mg/mL

技术

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: 1-2 μg/mL using HeLa or COS7 or CHO cell extracts

同位素/亚型

IgG2a

UniProt登记号

运输

dry ice

储存温度

−20°C

靶向翻译后修饰

unmodified

基因信息

相关类别

一般描述

Monoclonal Anti-U1 snRNP C (U1C) (rat IgG2a isotype) is derived from the hybridoma 4H12 produced by the fusion of mouse myeloma cells (SP2) and splenocytes from a rat immunized with mouse U1C protein. Small nuclear ribonucleoprotein polypeptide C (U1C) is mapped to human chromosome 6p21.31.
The U1 snRNP complex contains the U1 snRNA molecule and the U1 snRNP specific proteins U1-70K, U1A and U1C, plus a common set of eight proteins, called Sm proteins U1A and U1-70K contain RNA binding domains and interact with naked snRNA on their own.

特异性

Monoclonal Anti-U1 snRNP C (U1C) recognizes human, monkey, mouse, rat, and hamster U1C.

免疫原

mouse U1C protein fusion protein

应用

Anti-U1 snRNP C (U1C) antibody, Rat monoclonal has been used for:
  • immunoblotting
  • immunofluorescence
  • immunoprecipitation
  • immunocytochemistry

生化/生理作用

The U1 small nuclear ribonucleoprotein particle (snRNP) has an important function in the early formation of the spliceosome, the multicomponent complex in which pre-mRNA splicing takes place. The binding of U1C to the U1snRNP particle is dependent on protein-protein interactions between U1C and U1-70K as well as U1C and the common Sm proteins.
U1A and U1−70K contain RNA binding domains and interact with naked snRNA on their own. In cultured HeLa cells, mutant U1C proteins that are not able to bind to the U1 snRNP do not accumulate in the nucleus, indicating that nuclear accumulation of U1C is due to incorporation of the protein into the U1 snRNP.

外形

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

储存及稳定性

Store at -20 °C. For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze at -20 °C in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

免责声明

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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储存分类代码

12 - Non Combustible Liquids

WGK

nwg

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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分析证书(COA)

Lot/Batch Number

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访问文档库

Byung Ran So et al.
Molecular cell, 76(4), 590-599 (2019-09-17)
Full-length transcription in the majority of human genes depends on U1 snRNP (U1) to co-transcriptionally suppress transcription-terminating premature 3' end cleavage and polyadenylation (PCPA) from cryptic polyadenylation signals (PASs) in introns. However, the mechanism of this U1 activity, termed telescripting, is
Binkai Chi et al.
Nucleic acids research, 46(22), 11939-11951 (2018-11-07)
Understanding the molecular pathways disrupted in motor neuron diseases is urgently needed. Here, we employed CRISPR knockout (KO) to investigate the functions of four ALS-causative RNA/DNA binding proteins (FUS, EWSR1, TAF15 and MATR3) within the RNAP II/U1 snRNP machinery. We
Crystal structure of human spliceosomal U1 snRNP at 5.5 AA resolution
Krummel DA, et al.
Nature, 458(7237), 475-475 (2009)
Nuclear accumulation of the U1 snRNP-specific protein C is due to diffusion and retention in the nucleus
Gunnewiek J, et al.
Experimental Cell Research, 235(1), 265-273 (1997)
The splicing factor U1C represses EWS/FLI-mediated transactivation
Knoop LL and Baker SJ
Test, 275(32), 24865-24871 (2000)

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