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U4758

Sigma-Aldrich

Anti-U2AF65 antibody, Mouse monoclonal

clone MC3, purified from hybridoma cell culture

Synonym(s):

Anti-U2AF65

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

MC3, monoclonal

form

buffered aqueous solution

mol wt

antigen ~65 kDa

species reactivity

human, rat, Xenopus, mouse

packaging

antibody small pack of 25 μL

technique(s)

electron microscopy: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 0.1-0.2 μg/mL using total cell extract from HeLa cells

isotype

IgG2b

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... U2AF2(11338)
mouse ... U2af2(22185)
rat ... U2af2(308335)

General description

Monoclonal Anti-U2AF65 (mouse IgG2b isotype) is derived from the MC3 hybridoma produced by the fusion of mouse myeloma cells (Ag8.653 cells) and splenocytes from BALB/c mice immunized with recombinant human U2AF65. U1, U2, U4/U6, and U5 are small nuclear riboprotein (snRNPs) that are major subunits of spliceosomes. Spliceosomes also contain non snRNPs proteins such as alternative splicing factor/splicing factor 2 (ASF/SF2), 35 kDa spliceosomal component (SC-35) and U2 snRNP auxiliary splicing factor (U2AF). U2 snRNP auxiliary factor 65 kDa (U2AF65) is a splicing factor which has three C-terminal RNA recognition motifs (RRMs) and an N-terminal arginine/serine-rich (RS) domain. This gene is mapped to human chromosome 19q13.42. Splicing factor U2AF65kDa subunit is a non-snRNP protein component of spliceosome complexes.

Immunogen

recombinant human U2AF65.

Application

Monoclonal Anti-U2AF65 antibody produced in mouse has been used in:
  • RNA immunoprecipitation
  • immunoblotting
  • chromatin immunoprecipitation (ChIP)
  • enzyme-linked immunosorbent assay (ELISA)
  • immunohistochemistry
  • immunocytochemistry
  • immunoelectron microscopy

Biochem/physiol Actions

U2 snRNP auxiliary factor 65 kDa (U2AF65)/U2AF2 helps to supply the small nuclear ribonucleoprotein (snRNP) U2, which is subunit of the spliceosome. It can induce the exclusion of alternative exons. U2AF65 primarily regulates the splicing of pre-mRNA. The serine-rich (RS) repeats at the N-terminal region act as a signalling factor for nuclear localization. (U2AF65) and (U2AF35) are components of the splicing factor U2AF that transports between the cytoplasm and the nucleus.

Physical form

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

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

10 - Combustible liquids

WGK

WGK 2

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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Gloria Barbarani et al.
Scientific reports, 7(1), 14088-14088 (2017-10-28)
The Sox6 transcription factor is crucial for terminal maturation of definitive red blood cells. Sox6-null mouse fetuses present misshapen and nucleated erythrocytes, due to impaired actin assembly and cytoskeleton stability. These defects are accompanied with a reduced survival of Sox6
In vitro iCLIP-based modeling uncovers how the splicing factor U2AF2 relies on regulation by cofactors
Sutandy FXR, et al.
Genome Research, 28(5), 699-713 (2018)
Splicing inhibition of U2AF65 leads to alternative exon skipping
Cho S, et al.
Proceedings of the National Academy of Sciences of the USA, 112(32), 9926-9931 (2015)
Spliceosome structure and function
Will CL and Luhrmann R
Cold Spring Harbor Perspectives in Biology, 3(7), a003707-a003707 (2011)
The role of splicing factor mutations in the pathogenesis of the myelodysplastic syndromes
Boultwood J, et al.
Advances in Biological Regulation, 54(32), 153-161 (2014)

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