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DOK3 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q7L591 |
|---|---|
| Clone Names | 101008016 |
| Gene ID | 79930 |
|---|---|
| Other Names | Docking protein 3, Downstream of tyrosine kinase 3, DOK3 |
| 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 | DOK3 |
|---|---|
| Function | DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL1 function (By similarity). |
| Cellular Location | Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side |
| Tissue Location | Expressed in spleen.. |
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
DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate Abl function (By similarity).
References
Berger, A.H., et al. Nat. Genet. 42(3):216-223(2010)Senis, Y.A., et al. J. Thromb. Haemost. 7(10):1718-1726(2009)Honma, M., et al. Genes Cells 11(2):143-151(2006)Robson, J.D., et al. Mol. Cell. Biol. 24(6):2332-2343(2004)Favre, C., et al. Genes Immun. 4(1):40-45(2003)
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