Hi Ruben,

I know you were asking for advice based on personal experience, but I thought I'd like to bring BenchSci to your attention (https://www.benchsci.com)

Please see attached for more info. You might be interested in exploring the PTM filter for a specific phosphorylated form of GluR1/2

I hope this helps!

Maurice

I have searched for GluR in my protein database of liver cells (please see file; HepG2 fucoidan).

Healed hepatocyte HepG2 (cultured with fucoidan) has GluR7/GluK3/Glutamate receptor ionotropic, kainate 3/Excitatory amino acid receptor 5 at 2.2 μg/mg of cell protein.

LC tissue (named as No.6) has GluN2A/Glutamate receptor ionotropic, NMDA 2A/N-Methyl D-aspartate receptor subtype 2A/NR2A/NMDAR2A at 1.8 μg/mg of tissue protein.

Glycine receptor alpha2 chain is detectable only HCC tissue (No.6) at 6.6 μg/mg of tissue protein.

GluR and GlyR seem to be rarely expressed protein although brain tissue has not been searched. I do not understand why only glycine, L-glutamic acid, and D-serine have become to neurotransmitter.

Further, hydrophobic membrane proteins are difficult to be analyzes by SDS-PAGE and western blotting (my unpublished experience, please see file; IEF for hydrophobic proteins). Therefore, I must have to develop the detection and identification method for the protein expression chemically by using famous Edman degradation reaction (please see again file; HepG2 fucoidan). This quantitative PDMD (protein-direct-microsequencing-deciphering) method is superior especially onto membrane proteins to unreliable SDS-PAGE, western blot, and immuno assays.