HSPB2 Human
Description
HSPB2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Heat Shock 27kDa Protein 2 (HSP27), also known as HSPB1, is a member of the small heat shock protein (sHSP) family. These proteins are highly conserved across species and play crucial roles in cellular protection against stress. HSP27 is particularly notable for its involvement in protein folding, protection against apoptosis, and regulation of the cytoskeleton.
HSP27 was initially characterized in response to heat shock, a condition where cells are exposed to elevated temperatures. The protein was found to act as a molecular chaperone, facilitating the proper refolding of damaged proteins . Over time, research revealed that HSP27 responds to various stress conditions, including oxidative and chemical stress .
HSP27 belongs to the small molecular weight heat shock protein family, which ranges from 12 to 43 kDa . It shares a conserved C-terminal domain known as the α-crystallin domain, which is also found in the vertebrate eye lens α-crystallin . This domain is essential for the protein’s oligomerization, a process crucial for its function .
HSP27 is a multifunctional protein with several roles:
- Protein Chaperone: It assists in the proper folding of nascent and stress-denatured proteins, preventing their aggregation .
- Antioxidant: During oxidative stress, HSP27 lowers reactive oxygen species (ROS) levels by increasing intracellular glutathione and reducing intracellular iron .
- Anti-apoptotic: HSP27 inhibits apoptosis by interacting with both mitochondrial-dependent and independent pathways . It binds to DAXX during Fas-FasL mediated apoptosis, preventing the binding of Ask1 by DAXX . It also interacts with Bax and cytochrome c, preventing mitochondrial-dependent apoptosis .
- Cytoskeletal Regulation: HSP27 regulates actin cytoskeletal dynamics, promoting actin polymerization and functioning as an actin capping protein .
HSP27 has been implicated in various disease states, playing both protective and counter-protective roles. It is involved in renal injury, fibrosis, cancer, neurodegenerative diseases, and cardiovascular diseases . Its anti-apoptotic properties have significant implications for the success of certain chemotherapies .
Recombinant HSP27 is produced using genetic engineering techniques, where the HSP27 gene is inserted into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the protein, which can be used for research and therapeutic purposes.
