|Other Names||Cysteine and histidine-rich domain-containing protein 1, CHORD domain-containing protein 1, CHORD-containing protein 1, CHP-1, Protein morgana, CHORDC1, CHP1|
|Target/Specificity||The synthetic peptide sequence is selected from aa 142-156 of HUMAN CHORDC1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|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.|
|Function||Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Involved in stress response. Prevents tumorigenesis.|
|Tissue Location||Underexpressed in many breast and lung cancers.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent 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.
CHORDC1 may be play a role in the regulation of NOD1 via its interaction with HSP90AA1 (By similarity).
Gano, J.J., et al. Mol. Cell Proteomics 9(2):255-270(2010)
Lamesch, P., et al. Genomics 89(3):307-315(2007)
Wu, J., et al. FEBS Lett. 579(2):421-426(2005)
Brancaccio, M., et al. FEBS Lett. 551 (1-3), 47-52 (2003) :
Shirasu, K., et al. Cell 99(4):355-366(1999)
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