HSP70 Light

Ref. 3D-CRB1000373

Informations sur le produit

• Nom: HSP70 Light
• Synonymes: H-VTHAVVTVPAYFNDAQR-OH
• Marque: Biosynth
• Description: Glucose-regulated protein 78 kDa (GRP78) is a member of the 70 kDa heat shock protein (HSP70) family and is evolutionarily conserved from yeast to humans. GRP78 contains several domains that are crucial for its function and localisation. As a molecular chaperone, GRP78 contains an ATPase domain and a substrate-binding domain, which facilitate folding of nascent peptides in the ER. GRP78 also acts as a key regulator of unfolded protein response (UPR). In non-stressed cells, GRP78 maintains the three transmembrane UPR sensors (PERK, IRE1 and ATF6) inactive through direct binding. Upon ER stress, accumulated misfolded proteins titrate GRP78 away, releasing UPR sensors and leading to activation of UPR signals. GRP78 is a potent anti-apoptotic protein. This could be in part due to the ability of GRP78 to form a complex with and sequester procaspase-7, an executioner caspase and BIK, a pro-apoptotic member of the Bcl-2 family, both of which are located at the outer surface of the ER.In cancer, up-regulation of GRP78 is widely observed and associated with aggressive growth and invasiveness. While GRP78 is traditionally regarded as an ER luminal protein, studies have emerged which show that GRP78 can be detected in other cellular compartments including cell surface, cytosol, nucleus, and mitochondria. Unlike its role in the ER in processing and folding of nascent proteins, GRP78 exhibits different functions on the cell surface, where it regulates critical oncogenic signalling.The discovery that GRP78 is preferentially expressed on the surface of cancer cells, but not normal organs in vivo, opens a promising strategy for tumour specific targeting. However, the mechanisms for stress-induced translocation of GRP78 to the cell surface are just emerging.

Propriétés chimiques

• Masse moléculaire: 1,887 g/mol
• Degré de pureté: Min. 95%