SAB4200188
Anti-U1 snRNP C (U1C) antibody, Rat monoclonal
clone 4H12, purified from hybridoma cell culture
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Synonym(s):
Anti-Snrp1c, Anti-Snrpc, Anti-U1 small nuclear ribonucleoprotein C, Anti-U1-C, Anti-U1C
UNSPSC Code:
12352203
NACRES:
NA.41
Recommended Products
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
human ... SNRPC(6631)
mouse ... Snrpc(20630)
rat ... LOC685273(685273)
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.
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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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
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)
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)
U1 snRNP protects pre-mRNAs from premature cleavage and polyadenylation
Kaida D, et al.
Nature, 468(7324), 664-664 (2010)
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