|Other Names||Hypoxia up-regulated protein 1, 150 kDa oxygen-regulated protein, ORP-150, 170 kDa glucose-regulated protein, GRP-170, HYOU1, GRP170, ORP150|
|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||Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding.|
|Cellular Location||Endoplasmic reticulum lumen.|
|Tissue Location||Highly expressed in tissues that contain well- developed endoplasmic reticulum and synthesize large amounts of secretory proteins. Highly expressed in liver and pancreas and lower expression in brain and kidney. Also expressed in macrophages within aortic atherosclerotic plaques, and in breast cancers|
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Provided below are standard protocols that you may find useful for product applications.
HYOU1 belongs to the heat shock protein 70 family. The protein is thought to play an important role in protein folding and secretion in the ER. Since suppression of the protein is associated with accelerated apoptosis, it is also suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein has been shown to be up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor invasiveness. This signal peptide-lacking protein, which is only 3 amino acids shorter than the mature protein in the ER, is thought to have a housekeeping function in the cytosol. In rat, this protein localizes to both the ER by a carboxy-terminal peptide sequence and to mitochondria by an amino-terminal targeting signal.
Kitao,Y., Matsuyama,T. Antioxid. Redox Signal. 9 (5), 589-595 (2007)Bando,Y., Ogawa,S. Am. J. Physiol., Cell Physiol. 278 (6), C1172-C1182 (2000)
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