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PDZ11 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q5EBL8 |
|---|---|
| Clone Names | 80220159 |
| Gene ID | 51248 |
|---|---|
| Other Names | PDZ domain-containing protein 11, ATPase-interacting PDZ protein, Plasma membrane calcium ATPase-interacting single-PDZ protein, PMCA-interacting single-PDZ protein, PDZD11, AIPP1, PDZK11, PISP |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7791a was selected from the N-term region of human PDZ11. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | PDZD11 |
|---|---|
| Synonyms | AIPP1, PDZK11, PISP |
| Function | Mediates docking of ADAM10 to zonula adherens by interacting with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10- binding protein TSPAN33. |
| Cellular Location | [Isoform 2]: Secreted. |
| Tissue Location | Widely expressed (at protein level). |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
PDZ domains are modular protein interaction domains that often occur in scaffolding proteins that bind in a sequence-specific fashion the C-terminal peptide sequence or at times the internal peptide sequences of target proteins.
References
Stephenson,S.E., J. Biol. Chem. 280 (39), 33270-33279 (2005)Goellner,G.M., Ann. N. Y. Acad. Sci. 986, 461-471 (2003)
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