84-5899-83　HSPD1 100ul　565201

特徴

• Chaperonin implicated in mitochondrial protein import and macromolecular assembly.
• Together with Hsp10, facilitates the correct folding of imported proteins.
• May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:1346131, PubMed:11422376).
• The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring.
• In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10.
• This leads to sequestration of the substrate protein in the inner cavity ofHsp60 where, for a certain period of time, it can fold undisturbed by other cell components.
• Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
• Applications:Suitable for use in ELISA, Western Blot and Immunohistochemistry.
• Other applications not tested.
• Recommended Dilutions:Western Blot: 1:1000-1:5000Immunohistochemistry (Paraffin): 1:200-1:500.
• Heat antigen retrieval is required using citrate buffer, pH 6.0
• Optimal dilutions to be determined by the researcher.
• Storage and Stability:May be stored at 4°C for short-term only.
• Aliquot to avoid repeated freezing and thawing.
• Store at -20°C.
• Aliquots are stable for 12 months after receipt.
• For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.