HSP27 Mouse
Greater than 90.0% as determined by SDS-PAGE.
Description
HSP27 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-209 a.a) and having a molecular mass of 25.4kDa. HSP27 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MGSMTERRVP FSLLRSPSWE PFRDWYPAHS RLFDQAFGVP RLPDEWSQWF SAAGWPGYVR PLPAATAEGP AAVTLAAPAF SRALNRQLSS GVSEIRQTAD RWRVSLDVNH FAPEELTVKT KEGVVEITGK HEERQDEHGY ISRCFTRKYT LPPGVDPTLV SSSLSPEGTL TVEAPLPKAV TQSAEITIPV TFEARAQIGG PEAGKSEQSG AK.
Product Science Overview
Heat Shock Protein 27 (HSP27), also known as HSPB1, is a small heat shock protein that plays a crucial role in cellular stress responses. In mice, the recombinant form of this protein is often used in research to study its functions and potential therapeutic applications. This article delves into the background, structure, functions, and significance of HSP27, particularly focusing on its recombinant form in mice.
HSP27 belongs to the small heat shock protein (sHsp) family, which includes proteins with molecular weights ranging from 12 to 43 kDa . These proteins share a conserved C-terminal domain known as the α-crystallin domain, which is essential for their chaperone activity . The α-crystallin domain consists of 80 to 100 amino acid residues and forms β-sheets that are crucial for the formation of stable dimers .
One unique feature of HSP27 is the presence of a cysteine residue at the dimer interface within the α-crystallin domain. This cysteine can form a disulfide bond, linking the dimers covalently . The N-terminal region of HSP27 contains a less conserved WD/EPF domain, followed by a short variable sequence . The C-terminal region, despite its low sequence conservation, contains a locally conserved Ile-Xxx-Ile/Val (IxI/V) motif that regulates the assembly of oligomers .
HSP27 performs several critical functions in the cell, primarily related to its role as a molecular chaperone. It helps in the proper folding of proteins, preventing aggregation and assisting in the refolding of denatured proteins . This chaperone activity is vital for maintaining cellular proteostasis, especially under stress conditions.
Additionally, HSP27 acts as an antioxidant by reducing reactive oxygen species (ROS) levels and increasing intracellular glutathione levels . It also plays a significant role in inhibiting apoptosis by interacting with various apoptotic pathways. For instance, HSP27 binds to DAXX during Fas-FasL mediated apoptosis, preventing the binding of Ask1 by DAXX . It also interacts with Bax and cytochrome c, inhibiting mitochondrial-dependent apoptosis .
HSP27 is involved in actin cytoskeletal remodeling, promoting actin polymerization and functioning as an actin capping protein . This activity is crucial for maintaining cell shape, motility, and division.
The recombinant form of HSP27 in mice is extensively used in research to understand its functions and potential therapeutic applications. Studies have shown that HSP27 is implicated in various disease states, including renal injury, fibrosis, cancer, neurodegenerative diseases, and cardiovascular diseases . Its role as a biomarker and therapeutic target is of particular interest in these contexts.
