Recombinant Human FKBP11 protein (Fc Chimera)

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FKBP11 also known as FK506 binding protein 11 or FK506-binding protein-like is an immunophilin with peptidyl-prolyl isomerase activity. It facilitates protein folding by accelerating protein folding through cis-trans isomerization of proline residues. The molecular weight of FKBP11 is approximately 19.8 kDa. This protein is primarily expressed in the endoplasmic reticulum and shows high expression levels in immune-related tissues such as the spleen and lymph nodes.

Biological function summary

FKBP11 plays a role in maintaining protein homeostasis in the cellular environment. It is involved in the folding and maturation of proteins particularly those that are endoplasmic reticulum-resident. FKBP11 is part of the tetratricopeptide repeat (TPR)-containing immunophilin family which often interacts with other proteins and complexes within the endoplasmic reticulum to assist in protein quality control and trafficking.

Pathways

FKBP11 participates in the unfolded protein response (UPR) which is an essential cellular pathway for managing stress related to misfolded proteins in the endoplasmic reticulum. It is also involved in the protein-folding pathway alongside other chaperones and peptidyl-prolyl isomerases including cyclophilins and other FK506-binding proteins. FKBP11 has functional interactions with key molecules such as HSP90 which is an important chaperone in protein maintenance.

FKBP11 has implications in conditions related to protein misfolding and endoplasmic reticulum stress including neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. Aberrant expression or malfunction of FKBP11 can influence the progression of these disorders through its interaction with protein complexes involved in protein aggregation and neurotoxicity. FKBP11 indirectly connects to proteins like tau and α-synuclein which are central to the pathogenic processes of these neurological diseases.