The SDF2 gene encodes a protein that is believed to be a secretory protein. It has regions of similarity to hydrophilic segments of yeast mannosyltransferases . The human recombinant form of SDF2 is produced in E. coli and consists of a single, non-glycosylated polypeptide chain containing 216 amino acids, with a molecular mass of approximately 23.7 kDa .
SDF2 is involved in the endoplasmic reticulum (ER) stress response and protein folding. It is part of the chaperone complex that assists in the proper folding of newly synthesized proteins and the refolding of misfolded proteins . This function is crucial for maintaining cellular homeostasis and preventing the accumulation of misfolded proteins, which can lead to various diseases.
While the exact clinical implications of SDF2 are still being studied, its role in protein folding and ER stress response suggests that it could be involved in conditions related to protein misfolding and aggregation. These conditions include neurodegenerative diseases such as Alzheimer’s and Parkinson’s disease.
Recombinant human SDF2 is used in various research applications to study its function and potential therapeutic uses. Its role in the ER stress response makes it a target of interest for developing treatments for diseases caused by protein misfolding.