The cookie settings on this website are set to 'allow all cookies' to give you the very best experience. Please click Accept Cookies to continue to use the site.
Heat shock proteins (HSPs)/stress proteins are molecular chaperones that are induced by various environmental and physiological stimuli. The 150-kDa oxygen-regulated protein (ORP150), a new member of HSP family, functions as a molecular chaperone in the endoplasmic reticulum (1). It is reported that the ORP150 is an integral participant in ischemic cytoprotective pathways. (2). And, the ORP150 is expressed in human wounds along with VEGF. Colocalization of these two molecules was observed in macrophages in the neovasculature, suggesting a role of ORP150 in the promotion of angiogenesis (3). Furthermore, ORP150 is up-regulated in tumors and, in breast tumors, may be associated with tumor invasiveness. For research use only, not for use in diagnostic procedures.
Heat shock proteins (HSPs)/stress proteins are molecular chaperones that are induced by various environmental and physiological stimuli. The 150-kDa oxygen-regulated protein (ORP150), a new member of HSP family, functions as a molecular chaperone in the endoplasmic reticulum (1). It is reported that the ORP150 is an integral participant in ischemic cytoprotective pathways. (2). And, the ORP150 is expressed in human wounds along with VEGF. Colocalization of these two molecules was observed in macrophages in the neovasculature, suggesting a role of ORP150 in the promotion of angiogenesis (3). Furthermore, ORP150 is up-regulated in tumors and, in breast tumors, may be associated with tumor invasiveness. For research use only, not for use in diagnostic procedures.