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R3902

Sigma-Aldrich

Monoclonal Anti-hnRNP M1-M4 antibody produced in mouse

clone HL374 (1D8-2C5), purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-heterogeneous nuclear ribonucleoprotein M1-M4

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About This Item

MDL number:
MFCD03845440
UNSPSC Code:
12352203

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

HL374 (1D8-2C5), monoclonal

form

buffered aqueous solution

species reactivity

human, pig, mouse, rat, bovine, rabbit

technique(s)

immunoprecipitation (IP): suitable
western blot: 0.05-0.1 μg/mL using total extracts of human A431 cells

isotype

IgG1

UniProt accession no.

P52272

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... HNRNPM(4670)
mouse ... Hnrnpm(76936)
rat ... Hnrpm(116655)

Immunogen

hnRNP M1-4 (M19 fusion protein).

Physical form

Supplied as a 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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Certificates of Analysis (COA)

Lot/Batch Number
082K4803

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K V Datar et al.
Nucleic acids research, 21(3), 439-446 (1993-02-11)
Recent reports indicate that proteins which directly bind to nascent RNA polymerase II transcripts, the heterogeneous nuclear ribonucleoproteins (hnRNPs), play an important role in both transcript-specific packaging and alternative splicing of pre-mRNAs. Here we describe the isolation and characterization of
Ivo A Hendriks et al.
Nature structural & molecular biology, 21(10), 927-936 (2014-09-15)
SUMOylation is a reversible post-translational modification essential for genome stability. Using high-resolution MS, we have studied global SUMOylation in human cells in a site-specific manner, identifying a total of >4,300 SUMOylation sites in >1,600 proteins. To our knowledge, this is
Joost Schimmel et al.
Molecular & cellular proteomics : MCP, 7(11), 2107-2122 (2008-06-21)
Many proteins are regulated by a variety of post-translational modifications, and orchestration of these modifications is frequently required for full control of activity. Currently little is known about the combinatorial activity of different post-translational modifications. Here we show that extensive

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