FK506 Binding Protein 14 (FKBP14) is a member of the FK506-binding protein (FKBP) family, which is known for its role in immunoregulation and protein folding. FKBPs are peptidyl-prolyl isomerases (PPIases) that catalyze the cis-trans isomerization of proline residues in polypeptides, a process crucial for proper protein folding and function. FKBP14, in particular, has been identified as an endoplasmic reticulum (ER)-resident protein involved in various cellular processes, including protein folding and trafficking .
FKBP14 is a 22-kDa protein that contains a peptidyl-prolyl isomerase domain, two EF-hand motifs, and an ER retention signal . The PPIase domain is responsible for its isomerase activity, which is similar to that of other FKBPs and cyclophilins. FKBP14’s role in the ER suggests it is involved in the quality control of newly synthesized proteins, ensuring they are correctly folded before being transported to their final destinations.
Mutations in the FKBP14 gene have been linked to various diseases, including Ehlers-Danlos syndrome, a connective tissue disorder characterized by hypermobility, skin hyperextensibility, and tissue fragility . The involvement of FKBP14 in such diseases highlights its importance in maintaining cellular and tissue integrity.
Mouse anti-human FKBP14 antibodies are monoclonal antibodies developed to specifically target and bind to the human FKBP14 protein. These antibodies are used in various research applications, including Western blotting, immunohistochemistry, and immunoprecipitation, to study the expression and function of FKBP14 in different tissues and under various conditions.
The use of mouse anti-human FKBP14 antibodies has facilitated numerous studies aimed at understanding the role of FKBP14 in health and disease. For example, these antibodies have been used to investigate the expression patterns of FKBP14 in different tissues, its involvement in protein folding and trafficking, and its role in disease pathogenesis. Additionally, these antibodies have been instrumental in identifying potential therapeutic targets for diseases associated with FKBP14 dysfunction.