HSPB9 Human
Description
HSPB9 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Heat Shock Protein B9 (HSPB9), also known as CT51, is a member of the small heat shock protein (HSP20) family. These proteins are known for their role in protecting cells from stress by acting as molecular chaperones. HSPB9 is specifically expressed in the testis and localizes to both the cytoplasm and nucleus .
HSPB9 is a small protein with a molecular weight of approximately 19.6 kDa. It consists of 159 amino acids and is characterized by the presence of a conserved alpha-crystallin domain, which is typical of small heat shock proteins . The primary function of HSPB9, like other heat shock proteins, is to assist in the proper folding of proteins, prevent protein aggregation, and protect cells from stress-induced damage.
Recombinant human HSPB9 is produced using bacterial expression systems, typically Escherichia coli (E. coli). The recombinant protein is often tagged with a His-tag at the N-terminus to facilitate purification. The production process involves cloning the HSPB9 gene into an expression vector, transforming the vector into E. coli, and inducing protein expression. The recombinant protein is then purified using affinity chromatography techniques .
Heat shock proteins, including HSPB9, play crucial roles in cellular homeostasis and stress response. They are involved in various cellular processes such as protein folding, assembly, translocation, and degradation. HSPB9, in particular, has been implicated in the regulation of apoptosis and cellular stress responses. Its expression is upregulated in response to various stress conditions, including heat shock, oxidative stress, and exposure to toxic substances .
HSPB9 and other heat shock proteins have gained significant attention in the field of cancer research. Tumor cells often exhibit elevated levels of heat shock proteins, which contribute to their survival, proliferation, and resistance to apoptosis. As a result, heat shock proteins, including HSPB9, are being explored as potential targets for cancer therapy. Additionally, recombinant HSPB9 is used in research to study its role in cellular stress responses and its potential therapeutic applications .
