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MABS2030

Sigma-Aldrich

Anti-IRP2 Antibody, clone 3B11

clone 3B11, from mouse

Synonym(s):

Iron-responsive element-binding protein 2, IRE-BP 2, Iron regulatory protein 2

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

3B11, monoclonal

species reactivity

mouse, human

packaging

antibody small pack of 25 μg

technique(s)

immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgGκ

NCBI accession no.

UniProt accession no.

target post-translational modification

unmodified

Gene Information

human ... IREB2(3658)

General description

Iron-responsive element-binding protein 2 (UniProt: P48200; also known as IRE-BP 2, Iron regulatory protein 2, IRP2) is encoded by the IREB2 gene (Gene ID: 3658) in human. IRP2 is a member of the aconitase/IPM isomerase family that serves as an RNA-binding protein, which regulates the homeostatic binding of intracellular iron to its specific cognate mRNA hairpin structures known as iron-responsive elements (IREs). Its interaction with IRE is shown to be abolished under conditions of high iron. In iron rich cells and in the presence of oxygen, IRP2 is ubiquitinated and degraded in proteasome pathway. Its ubiquitination is achieved by a SCF complex containing FBXL5. Upon iron and oxygen depletion FBXL5 is degraded, preventing ubiquitination and allowing its RNA-binding activity. IN IRP2, Cys201 and His204 have been shown to be critical for IRP2 degradation. Cys201 binds ferric heme and His204 binds ferrous heme and they are involved in sensing the redox state of the heme iron and in generation the oxidative modification. Two isoforms of IRP2 have been described that are produced by alternative splicing. (Ref.: Ashizuka, M., et al. (2002). Mol. Cell. Biol. 22(18); 6375-6383; Ishikawa, H., et al. (2005). Mol. Cell 19(2); 171-181).

Specificity

Clone 3B11 is a mouse monoclonal antibody that detects Iron regulatory protein 2 (IRP2). It targets an epitope with in 73 amino acids from the N-terminal region.

Immunogen

GST-tagged recombinant fragment corresponding to 73 amino acids from the N-terminal region of human Iron regulatory protein 2 (IRP2).

Application

Anti-IRP2, clone 3B11 , Cat. No. MABS2030, is a mouse monoclonal antibody that detects Iron-responsive element-binding protein 2 and has been tested for use in Immunohistochemistry (Paraffin), Immunoprecipitation, and Western Blotting.
Immunoprecipitation Analysis: A representative lot immunoprecipitated IRP2 in Immunoprecipitation applications (Ashizuka, M., et. al. (2002). Mol Cell Biol. 22(18):6375-83).

Western Blotting Analysis: A representative lot detected IRP2 in Western Blotting applications (Yoshinaga, M., et. al. (2017). Cell Rep. 19(8):1614-1630).
Research Category
Signaling

Quality

Evaluated by Immunohistochemistry (Paraffin) in human kidney tissue sections.

Immunohistochemistry (Paraffin) Analysis: A 1:50 dilution of this antibody detected IRP2 in human kidney tissue sections.

Target description

105.06 kDa calculated.

Physical form

Format: Purified
Protein G purified
Purified mouse monoclonal antibody IgG in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Other Notes

Concentration: Please refer to lot specific datasheet.

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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Masanori Yoshinaga et al.
Cell reports, 19(8), 1614-1630 (2017-05-26)
Iron metabolism is regulated by transcriptional and post-transcriptional mechanisms. The mRNA of the iron-controlling gene, transferrin receptor 1 (TfR1), has long been believed to be negatively regulated by a yet-unidentified endonuclease. Here, we show that the endonuclease Regnase-1 is critical

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