HSPA13 Human
Description
HSPA13 is fused to a 40 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
DLAVVTGVAI QAGIDGGFWP LQVSALEIPN KHLQKTNFN.
Product Science Overview
Heat shock proteins (HSPs) are a family of proteins that are produced by cells in response to stressful conditions. They play a crucial role in protein folding, repair, and protection against cellular stress. Among these, the Heat Shock 70kDa Protein 13 (HSPA13), also known as the 70 kilodalton heat shock protein, is a significant member of the HSP70 family. This protein is highly conserved across different species and is involved in various cellular processes, including protein folding, protection against stress, and antigen transport.
The discovery of heat shock proteins dates back to the 1960s when Ferruccio Ritossa observed an unusual “puffing pattern” in the chromosomes of Drosophila (fruit flies) subjected to elevated temperatures. This phenomenon was later identified as the “Heat Shock Response,” leading to the identification of heat shock proteins .
HSPA13, like other members of the HSP70 family, consists of three major functional domains:
- N-terminal ATPase domain: This domain binds and hydrolyzes ATP (Adenosine triphosphate) to ADP (Adenosine diphosphate), leading to conformational changes in the protein.
- Substrate-binding domain (SBD): This domain interacts with extended polypeptides as substrates.
- C-terminal domain: This domain contains an EEVD motif that participates in binding to co-chaperones and other HSPs .
HSPA13 is involved in several critical cellular functions:
- Protein Folding: It acts as a molecular chaperone, assisting in the proper folding of nascent and stress-accumulated misfolded proteins.
- Stress Response: It helps protect cells from the adverse effects of physiological stresses such as heat, toxins, and heavy metals.
- Antigen Transport: During nutrient stress, HSPA13 participates in antigen transport to regulate MHC (major histocompatibility) class II presentation .
HSPA13 is ubiquitously expressed in various tissues and is upregulated in response to stress conditions. It is found in multiple cellular compartments, including the cytoplasm, endoplasmic reticulum, and extracellular exosomes . The expression of HSPA13 is tightly regulated at both transcriptional and post-transcriptional levels to ensure cellular homeostasis.
HSPA13 has been implicated in several diseases and conditions:
- Cancer: It is upregulated in cancer cells and is involved in protein homeostasis, contributing to cancer cell growth and survival .
- Neurodegenerative Diseases: Due to its role in protein folding and protection against stress, HSPA13 is being studied for its potential therapeutic applications in neurodegenerative diseases such as Alzheimer’s and Parkinson’s diseases.
