Analysis Note

ControlMouse heart tissue lysate

Application

Research Sub CategoryRNA Metabolism & Binding Proteins

Research CategoryEpigenetics & Nuclear Function

Anti-Fox1 Antibody, clone D8F8 is a Mouse Monoclonal Antibody for detection of Fox1 also known as hexaribonucleotide binding protein 1, Ataxin-2-binding protein 1 & has been validated in WB.

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.

General description

Fox1, also commonly referred to as Ataxin-2-binding protein 1, is an RNA binding protein involved in the regulation of tissue-specific alternative splicing. This protein contains a highly conserved RRM (RNA recognition motif) and associates with 5′-UGCAUGU-3′ elements. This protein has been demonstrated to regulate alternative splicing of tissue specific exons and differentially spliced exons during erythropoiesis. Its alternative name, Ataxin-2-binding protein, is a result of its association with the C terminus of ataxin 2 which may contribute to the pathology of the neurogenerative disease spinocerebellar ataxia type 2 (SCA2).

Immunogen

Recombinant protein corresponding to mouse Fox1.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Physical form

Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Protein G

Format: Purified

Quality

Evaluated by Western Blot in mouse heart tissue lysate.

Western Blot Analysis: 0.5 µg/mL of this antibody detected Fox1 on 10 µg of mouse heart tissue lysate.

Storage and Stability

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

Target description

~55 kDa observed. Uncharacterized bands potentially due to alternative splicing have been observed at ~33 and 37 kDa