SAB4200188
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
产品名称
Anti-U1 snRNP C (U1C) antibody, Rat monoclonal, clone 4H12, purified from hybridoma cell culture
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)
Application
Anti-U1 snRNP C (U1C) antibody, Rat monoclonal has been used for:
- immunoblotting
- immunofluorescence
- immunoprecipitation
- immunocytochemistry
Biochem/physiol Actions
Monoclonal Anti-U1 snRNP C (U1C) recognizes human, monkey, mouse, rat, and hamster U1C.
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.
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.
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.
Immunogen
mouse U1C protein fusion protein
Physical form
Solution in 0.01M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide
Preparation Note
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.
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存储类别
12 - Non Combustible Liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
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
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
The splicing factor U1C represses EWS/FLI-mediated transactivation
Knoop LL and Baker SJ
Test, 275(32), 24865-24871 (2000)
U1 snRNP protects pre-mRNAs from premature cleavage and polyadenylation
Kaida D, et al.
Nature, 468(7324), 664-664 (2010)
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
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