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Merck

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

分類程式碼代碼:
12352203
NACRES:
NA.41

生物源

rat

共軛

unconjugated

抗體表格

purified from hybridoma cell culture

抗體產品種類

primary antibodies

無性繁殖

4H12, monoclonal

形狀

buffered aqueous solution

分子量

~20 kDa

物種活性

human, mouse, rat, hamster, monkey

濃度

~1.0 mg/mL

技術

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

同型

IgG2a

UniProt登錄號

運輸包裝

dry ice

儲存溫度

−20°C

目標翻譯後修改

unmodified

基因資訊

一般說明

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.

特異性

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

免疫原

mouse U1C protein fusion protein

應用

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.

外觀

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

儲存和穩定性

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.

免責聲明

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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儲存類別代碼

12 - Non Combustible Liquids

水污染物質分類(WGK)

nwg

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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SMN2 splice modulators enhance U1--pre-mRNA association and rescue SMA mice
Palacino J, et al.
Nature Chemical Biology, 11(7), 511-511 (2015)
Interactome analyses revealed that the U1 snRNP machinery overlaps extensively with the RNAP II machinery and contains multiple ALS/SMA-causative proteins
Chi B, et al.
Scientific reports, 8(1), 8755-8755 (2018)
The splicing factor U1C represses EWS/FLI-mediated transactivation
Knoop LL and Baker SJ
Test, 275(32), 24865-24871 (2000)
Binkai Chi et al.
Scientific reports, 8(1), 8755-8755 (2018-06-10)
Mutations in multiple RNA/DNA binding proteins cause Amyotrophic Lateral Sclerosis (ALS). Included among these are the three members of the FET family (FUS, EWSR1 and TAF15) and the structurally similar MATR3. Here, we characterized the interactomes of these four proteins
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)

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