Ugrás a tartalomra
Merck

SAB4200188

Sigma-Aldrich

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

clone 4H12, purified from hybridoma cell culture

Szinonimák:

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

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
NACRES:
NA.41

biológiai forrás

rat

konjugátum

unconjugated

antitest forma

purified from hybridoma cell culture

antitest terméktípus

primary antibodies

klón

4H12, monoclonal

form

buffered aqueous solution

molekulatömeg

~20 kDa

faj reaktivitás

human, mouse, rat, hamster, monkey

koncentráció

~1.0 mg/mL

technika/technikák

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

izotípus

IgG2a

UniProt elérési szám

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

Általános leírás

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.

Egyediség

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

Immunogen

mouse U1C protein fusion protein

Alkalmazás

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

Biokémiai/fiziológiai hatások

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.

Fizikai forma

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

Tárolás és stabilitás

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.

Jogi nyilatkozat

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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Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

nwg

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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)
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)
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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