Description
Product Characteristics: Chaperonin 10, otherwise known as Cpn10, (groES in E.coli) make up a family of small heart shock proteins with an approximate molecular mass of 10 kDa (HSP10s). Cpn10 acts as a co-chaperone and interacts with the HSP60 family to promote proper folding of polypeptides. Cpn10 and Cpn60 both exhibit sevenfold axis of symmetry and function as a team in the protein folding and assembly process (1). Cpn10 has been located in human platelets, but is also present in human maternal serum (2, 3). It has been reported that human Cpn10 is identical with early pregnancy factor, which is involved in control over cell growth and development. This identification suggest that Cpn10 may act like a hormone in stressful situations such as pregnancy (4).
Target Information: This gene encodes a major heat shock protein which functions as a chaperonin. Its structure consists of a heptameric ring which binds to another heat shock protein in order to form a symmetric, functional heterodimer which enhances protein folding in an ATP-dependent manner. This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2. Naturally occurring read-through transcription occurs between this locus and the neighboring locus MOBKL3.[provided by RefSeq, Feb 2011]