Analysis Note

ControlHypothalamus tissue lysate

Application

Detect mGluR5 using this mouse monoclonal antibody, Anti-mGluR5 Antibody, clone N75/33 validated for use in western blotting & IHC.

Research CategoryNeuroscience

Western Blotting Analysis: 1 µg/mL from a representative lot detected mGluR5 in 10 µg of rat brain membrane tissue.

Immunohistochemistry Analysis: A 1:100 dilution from a representative lot detected mGluR5 in normal human midbrain tissue.

Research Sub CategorySynapse & Synaptic Biology

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

Metabotropic glutamate receptor 5 (mGluR5) is a G-protein mediated glutamate receptor that generates a calcium-activated chloride current. mGluR5 is widely distributed in neuronal cells of the central nervous system.

Immunogen

Recombinant protein corresponding to the C-terminus of rat mGluR5.

Epitope: C-terminus

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 Purified

Format: Purified

Quality

Evaluated by Western Blotting in mouse hypothalamus tissue lysate.

Western Blotting Analysis: 1 µg/mL of this antibody detected mGluR5 in 10 µg of mouse hypothalamus tissue lysate.

Specificity

This antibody recognizes the C-terminus of mGluR5. This antibody may cross react with mGluR1 based upon ﹤35% sequence homology.

Storage and Stability

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

Target description

~150-270 kDa observed. This protein may be observed at higher molecular weights due to glycosylation (Bhave, G., et al. (2003). J Biol Chem. 278(32):30294-30301). This protein is observed as a dimer at ~270 kDa, but is observed as a monomer at ~140 kDa under reduced conditions in SDS-PAGE (Romano, C., et al. (1996). J Biol Chem. 271(45):28612-28616.). Uncharacterized band(s) may be observed in some cell lysates.