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R5028

Sigma-Aldrich

Monoclonal Anti-hnRNP-C1/C2 antibody produced in mouse

clone 4F4, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-Heterogeneous Nuclear Ribonucleoprotein-C1/C2

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About This Item

MDL number:
MFCD06798703
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

4F4, monoclonal

form

buffered aqueous solution

mol wt

antigen 41 kDa
antigen 43 kDa

species reactivity

monkey, human, chicken, hamster

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 0.1-0.2 μg/mL using HeLa cell nuclear extract

isotype

IgG1

UniProt accession no.

P07910

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HNRNPC(3183)

General description

Monoclonal Anti-hnRNP-C1/C2 (mouse IgG1isotype) is derived from the 4F4 hybridoma produced by the fusion of mouse myeloma cells (SP2/0 cells) and splenocytes from BALB/c mice immunized with RNPs eluted from oligo (dT) cellulose column. Heterogeneous nuclear ribonucleoproteins C1/C2 (HnRNP C1/C2) are synthesized from C2 protein by alternative splicing and have an additional13-amino-acids. It is localized in nucleus and has leucine zipper-like RNA-binding motif. The hnRNP-C proteins have a single ribonucleoprotein (RNP) motif RNA-binding domain (RBD) of 80 to 100 amino acid long.

Immunogen

RNPs eluted from oligo (dT) cellulose column.

Application

Monoclonal Anti-hnRNP-C1/C2 antibody produced in mouse has been used in:
  • antibody microarray
  • western blotting
  • enzyme linked immunosorbent assay (ELISA)`
  • immunoprecipitation
  • immunocytochemistry

Biochem/physiol Actions

Heterogeneous nuclear ribonucleoproteins C1/C2(HnRNP C1/C2) is involved in protein translation, mRNA biogenesis and transport. The hnRNP-C proteins preferentially bind to uridine-rich RNA sequences. Oligomerization of the protein through leucine rich regions in its C-terminal end is important for RNA binding. Mutation of the hnRNPC gene is implicated in embryonic lethal phenotype.

Physical form

Solution in 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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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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Nathalie Meyer-Schaller et al.
Proceedings of the National Academy of Sciences of the United States of America, 106(30), 12365-12370 (2009-07-21)
Cullin (Cul)-based E3 ubiquitin ligases are activated through the attachment of Nedd8 to the Cul protein. In yeast, Dcn1 (defective in Cul neddylation 1 protein) functions as a scaffold-like Nedd8 E3-ligase by interacting with its Cul substrates and the Nedd8
A highly conserved SOX6 double binding site mediates SOX6 gene downregulation in erythroid cells
Cantu C, et al.
Nucleic Acids Research, 39(2), 486-501 (2010)
Nuclear efflux of heterogeneous nuclear ribonucleoprotein C1/C2 in apoptotic cells: a novel nuclear export dependent on Rho-associated kinase activation
Lee HH, et al.
Journal of Cell Science, 117(23), 5579-5589 (2004)
Role of human heterogeneous nuclear ribonucleoprotein C1/C2 in dengue virus replication
Dechtawewat T, et al.
Virology Journal, 12(1), 14-14 (2015)
The CCR4-NOT deadenylase complex controls Atg7-dependent cell death and heart function
Yamaguchi T, et al.
Science Signaling, 11(516), eaan3638-eaan3638 (2018)
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