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SAB4200188

Sigma-Aldrich

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

clone 4H12, purified from hybridoma cell culture

Synonym(s):

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

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rat

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

4H12, monoclonal

form

buffered aqueous solution

mol wt

~20 kDa

species reactivity

human, mouse, rat, hamster, monkey

concentration

~1.0 mg/mL

technique(s)

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

isotype

IgG2a

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

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.

Specificity

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

Immunogen

mouse U1C protein fusion protein

Application

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

Biochem/physiol Actions

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.

Physical form

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

Storage and Stability

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.

Disclaimer

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

12 - Non Combustible Liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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)
SMN2 splice modulators enhance U1--pre-mRNA association and rescue SMA mice
Palacino J, et al.
Nature Chemical Biology, 11(7), 511-511 (2015)
The splicing factor U1C represses EWS/FLI-mediated transactivation
Knoop LL and Baker SJ
Test, 275(32), 24865-24871 (2000)
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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