DOK5 Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9P104 |
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Clone Names | 4061501 |
Gene ID | 55816 |
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Other Names | Docking protein 5, Downstream of tyrosine kinase 5, Insulin receptor substrate 6, IRS-6, IRS6, DOK5, C20orf180 |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7693a was selected from the N-term region of human DOK5. 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 | DOK5 |
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Synonyms | C20orf180 |
Function | DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK5 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway. Putative link with downstream effectors of RET in neuronal differentiation. |
Tissue Location | Highest expression in skeletal muscle, lower in brain, heart and kidney. Also detected in activated peripheral blood T- lymphocytes. |
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Provided below are standard protocols that you may find useful for product applications.
Background
DOK5 is a member of the DOK family of membrane proteins, which are adapter proteins involved in signal transduction. The encoded protein interacts with phosphorylated receptor tyrosine kinases to mediate neurite outgrowth and activation of the MAP kinase pathway. In contrast to other DOK family proteins, this protein does not interact with RASGAP.
References
Cai, D., et al., J. Biol. Chem. 278(28):25323-25330 (2003).Favre, C., et al., Genes Immun. 4(1):40-45 (2003).
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