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Merck

SAB4200188

Sigma-Aldrich

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

clone 4H12, purified from hybridoma cell culture

Sinónimos:

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

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rat

conjugado

unconjugated

forma del anticuerpo

purified from hybridoma cell culture

tipo de anticuerpo

primary antibodies

clon

4H12, monoclonal

Formulario

buffered aqueous solution

mol peso

~20 kDa

reactividad de especies

human, mouse, rat, hamster, monkey

concentración

~1.0 mg/mL

técnicas

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

isotipo

IgG2a

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

Categorías relacionadas

Descripción general

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.

Especificidad

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

Inmunógeno

mouse U1C protein fusion protein

Aplicación

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

Acciones bioquímicas o fisiológicas

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.

Forma física

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

Almacenamiento y estabilidad

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.

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

nwg

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Visite la Librería de documentos

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
Crystal structure of human spliceosomal U1 snRNP at 5.5 AA resolution
Krummel DA, et al.
Nature, 458(7237), 475-475 (2009)
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
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)

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