HSPA6 Human
Description
HSPA6 human recombinant is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.
Product Specs
TTYSDNQPGV FIQVYEGERA MTKDNNLLGR FELSGIPPAP RGVPQIEVTF DIDANGILSV TATDRSTGKA NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA KNSLEAHVFH VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD.
Product Science Overview
Heat Shock 70kDa Protein 6 (HSPA6) is a member of the Heat Shock Protein 70 (HSP70) family, which is a group of highly conserved proteins that play a crucial role in cellular processes such as protein folding, trafficking, and prevention of aggregation . These proteins are known for their ability to protect cells from stress-induced damage by acting as molecular chaperones.
The concept of heat shock proteins was first discovered in the 1960s by Ferruccio Ritossa, who observed an unusual “puffing pattern” in the chromosomes of Drosophila (fruit flies) when exposed to elevated temperatures . This led to the identification of the Heat Shock Response and the subsequent discovery of Heat Shock Proteins (HSPs).
HSPA6, specifically, is a stress-inducible protein, meaning it is produced in response to cellular stressors such as heat, heavy metals, and other toxic chemicals . Unlike some other members of the HSP70 family, HSPA6 has little to no basal expression in most cells under normal conditions .
HSPA6, like other HSP70 proteins, consists of three major functional domains:
- N-terminal ATPase domain: This domain binds and hydrolyzes ATP (Adenosine triphosphate) to ADP (Adenosine diphosphate), driving conformational changes necessary for its chaperone activity.
- Substrate-binding domain (SBD): This domain interacts with extended polypeptides, helping in the proper folding of nascent proteins and the refolding of misfolded proteins.
- C-terminal domain: This domain contains an EEVD motif that is involved in binding to co-chaperones and other HSPs .
Recombinant HSPA6 is typically produced using bacterial or mammalian expression systems. The gene encoding HSPA6 is cloned into an expression vector, which is then introduced into host cells such as Escherichia coli or HEK293 cells. The recombinant protein is expressed, harvested, and purified using techniques such as affinity chromatography .
HSPA6 has significant potential in various biomedical applications. It is used in research to study cellular stress responses and protein folding mechanisms. Additionally, due to its role in protecting cells from stress-induced damage, HSPA6 is being explored for therapeutic applications, including cancer treatment and neurodegenerative diseases .
