HA211499

Product name:	Human HSP60/HSPD1, Tag Free
Catalog No.:	HA211499
Bio-Activity:	Testing in progress.
Purity:	>95% as determined by SDS-PAGE.
Endotoxin:	Less than 1.0 EU per μg by the LAL method.
Formulation:	Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4, 5% Trehalose, 5% mannitol.

Background:

HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 belong to a large class of molecules that assist protein folding, called molecular chaperones. Newly made proteins usually must fold from a linear chain of amino acids into a three-dimensional tertiary structure. The energy to fold proteins is supplied by non-covalent interactions between the amino acid side chains of each protein, and by solvent effects. Most proteins spontaneously fold into their most stable three-dimensional conformation, which is usually also their functional conformation, but occasionally proteins mis-fold. Molecular chaperones catalyze protein refolding by accelerating partial unfolding of misfolded proteins, aided by energy supplied by the hydrolysis of adenosine triphosphate (ATP). Chaperonin proteins may also tag misfolded proteins to be degraded.

Source:

HEK293

Storage:

Please avoid repeated freeze-thaw cycles. Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ It is recommended that aliquot the reconstituted solution to minimize freeze-thaw cycles.

Reconstitution:

Reconstitute at 250 μg/ml in sterile water.