PDZ domain scaffold protein anti-Human AMPA receptor GluR2
CAT#: SPD-L155
The PDZ domain that bound AMPA receptor GluR2 was isolated from the library using Phage display techonology. PDZ domains are modular protein-interaction domains that are specialized for binding to short peptide motifs at the extreme carboxy (C) termini of other proteins, athough they can also have other modes of interaction. After affinity maturation, PDZ domain variants were identified having affinities for AMPA receptor GluR2 as determined by biosensor technology. It's potential to be used in diagnostic, research and therapeutic applications.
Gene Expression
Normal Tissue
Figure 1 Cerebral cortex
Neuronal cells
Staining: Medium
Intensity: Strong
Quantity: <25%
Location: Cytoplasmic/membranous
Neuropil
Staining: High
Intensity: Strong
Quantity:>75%
Location: Cytoplasmic/membranous
* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/images/8441/166140_B_9_5.jpg
Normal Tissue
Figure 2 Hippocampus
Neuronal cells
Staining: Medium
Intensity: Strong
Quantity: <25%
Location: Cytoplasmic/membranous
* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/images/8441/166140_B_7_6.jpg
RNA Expression
Figure 3 RNA cell line category: Cell line enriched (SCLC-21H)
Cell lines ordered by descending RNA expression order.
* Image credit: Image credit: Human Protein Atlas v21.proteinatlas.org/ENSG00000120251-GRIA2
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Specifications
- Scaffold Name
- PDZ domain
- Origin
- PSD-95 protein
- Core Structure
- β-sheet
- Target
- AMPA receptor GluR2
- Species Reactivity
- Human
- Expression Host
- E. coli
- Applications
- ELISA; IHC; Microscopy; FC; WB; FuncS
Target
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Specific GluR2 Binder
Finding a specific binder for the AMPA receptor GluR2 subunit was challenging until we tested this PDZ domain. It works well in our biosensor assays, helping us study ligand-activated cation channels without interference from other subunits.
Relevant For ALS Research
We are researching the etiology of amyotrophic lateral sclerosis, specifically RNA editing at the Q/R site. This scaffold protein allows us to target and isolate the GRIA2 protein product to analyze its transmembrane domain properties.
Q&As
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What is the function of the GRIA2 target?
A: The gene product GRIA2 belongs to a family of glutamate receptors sensitive to AMPA. They function as ligand-activated cation channels. The GRIA2 subunit is subject to RNA editing which renders the channel impermeable to calcium ions.
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Is this product relevant to any specific disease research?
A: Yes, defective GRIA2 RNA editing at the Q/R site may be relevant to the etiology of amyotrophic lateral sclerosis (ALS). This PDZ domain scaffold, having affinities for AMPA receptor GluR2, is a valuable tool for investigating these mechanisms.
View the frequently asked questions answered by Creative Biolabs Support.
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Downloadable Resources
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Datasheet
MSDS
COA
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