Recombinant human FKBP14 protein is a Human Full Length protein, in the 20 to 211 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS, FuncS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
PPIase which accelerates the folding of proteins during protein synthesis. Has a preference for substrates containing 4-hydroxylproline modifications, including type III collagen. May also target type VI and type X collagens.
FKBP22, UNQ322/PRO381, FKBP14, Peptidyl-prolyl cis-trans isomerase FKBP14, PPIase FKBP14, 22 kDa FK506-binding protein, FK506-binding protein 14, Rotamase, 22 kDa FKBP, FKBP-22, FKBP-14
Recombinant human FKBP14 protein is a Human Full Length protein, in the 20 to 211 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS, FuncS.
pH: 7.4
Constituents: PBS, 10% Glycerol (glycerin, glycerine)
ab99328 is purified using conventional chromatography techniques.
PPIase which accelerates the folding of proteins during protein synthesis. Has a preference for substrates containing 4-hydroxylproline modifications, including type III collagen. May also target type VI and type X collagens.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
FKBP14 also known as FK506-binding protein 14 is a member of the FKBP family of proteins. It acts as a peptidyl-prolyl cis-trans isomerase assisting in the folding of certain proteins by accelerating the interconversion between proline residues. FKBP14 displays a molecular mass of approximately 23 kDa and is expressed in various tissues throughout the body including muscle and connective tissues. The protein typically resides in the endoplasmic reticulum where its main role involves assisting in protein folding processes ensuring proper cellular function.
FK506-binding protein 14 impacts protein assembly and stabilization. It participates in the modification and folding of newly synthesized proteins particularly collagens which are essential for maintaining structural integrity in tissues. FKBP14 does not operate as part of a larger complex but plays a significant role in maintaining the stability and functionality of extracellular matrix components. This activity highlights its importance in tissue homeostasis and cellular maintenance.
FKBP14 is integral to collagen biosynthesis and quality control pathways contributing to the structural framework of tissues. It influences the proper secretion and assembly of collagen types interacting with proteins like collagen type I through these processes. These pathways are critical for maintaining the extracellular matrix's structural properties ensuring that tissues correctly support cellular activities and organ architecture.
FKBP14 mutations or dysregulation connect to conditions like Bruck syndrome and Ehlers-Danlos syndrome. These diseases involve connective tissue abnormalities where defective collagen processing leads to impaired tissue integrity. Within Bruck syndrome FKBP14 directly relates to incorrect collagen modification which affects structural strength associating with proteins such as lysyl hydroxylase. Studying the interactions and functions of FKBP14 provides insight into these connective tissue disorders' underlying mechanisms and potential therapeutic targets.
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15% SDS-PAGE analysis of 3μg ab99328.
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