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Key Documents

R5028

Sigma-Aldrich

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

clone 4F4, purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

Anti-Heterogeneous Nuclear Ribonucleoprotein-C1/C2

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

4F4, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen 41 kDa
antigen 43 kDa

Espèces réactives

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

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... HNRNPC(3183)

Description générale

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.

Immunogène

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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)
hnRNP C is required for postimplantation mouse development but is dispensable for cell viability
Williamson DJ, et al.
Molecular and Cellular Biology, 20(11), 4094-4105 (2000)
The CCR4-NOT deadenylase complex controls Atg7-dependent cell death and heart function
Yamaguchi T, et al.
Science Signaling, 11(516), eaan3638-eaan3638 (2018)
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)
Séverine Cathelin et al.
The Journal of biological chemistry, 281(26), 17779-17788 (2006-04-26)
We have shown previously that caspases were specifically involved in the differentiation of peripheral blood monocytes into macrophages while not required for monocyte differentiation into dendritic cells. To identify caspase targets in monocytes undergoing macrophagic differentiation, we used the human

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