Recombinant Human FKBP14 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2096

Recombinant Human FKBP14 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2096
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Product Overview

Tag His
Host Species Human
Accession Q9NWM8
Synonym EDSKMH, FKBP22, IPBP12
Background FKBP14 belongs to the FK56-binding protein family. It contains 2 EF-hand domains and one PPIase FKBP-type domain. FKBP14 can be detected in the lumen of the endoplasmic reticulum where it is thought to accelerate the folding of proteins during protein synthesis. Truncation of the amino-terminus of FKBP14 significantly decreases peptidyl prolyl cis-trans isomerase activity, therefore implicating that the PPIase FKBP-type domain must be located at the N-terminus. Defects in FKBP14 can cause Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss. A syndrome with features of Ehlers-Danlos syndrome types VIA and VIB on the one hand, and the collagen VI-related congenital myopathies Ullrich congenital muscular dystrophy and Bethlem myopathy on the other hand.
Description A DNA sequence encoding the human FKBP14 (Q9NWM8) (Met1-Lys207) was expressed with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Ala 20
AA Sequence Met1-Lys207
Molecular Weight The recombinant human FKBP14 consists of 199 a.a. and predicts a molecular mass of 22.9 KDa. It migrates as an approximately 25 and 27 KDa band in SDS-PAGE under reducing conditions.
Purity (73.1+25.2)% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function 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.
Subcellular Location Endoplasmic reticulum lumen.
Database References
Associated Diseases Ehlers-Danlos syndrome, with progressive kyphoscoliosis, myopathy, and hearing loss (EDSKMH)

Gene Functions References

  1. FKBP14 may act as an oncogene through suppressing apoptosis and promoting motility in human cervical carcinogenesis. PMID: 28731139
  2. Genetic studies showed that the patient harboured a homozygous mutation (c.362dupC p.Glu122Argfs*7) in the FKBP14 gene, confirming kyphoscoliotic EDS related to this gene. PMID: 27905128
  3. FKBP14 may act as an oncogene in osteosarcoma via suppressing apoptosis and promoting invasion and adhesion in osteosarcoma carcinogenesis PMID: 27223089
  4. this report describes a potentially life-threatening vascular complication in early pediatric age and atlantoaxial instability, suggesting the need for FKBP14-related EDS patients of tailored follow-up that includes cardiovascular monitoring, that is, cerebral, thoracic and abdominal MRA, and cervical dynamic radiograph. PMID: 27149304
  5. observed changes in activity of six rER-resident PPIases, cyclophilin B (encoded by the PPIB gene), FKBP13 (FKBP2), FKBP19 (FKBP11), FKBP22 (FKBP14), FKBP23 (FKBP7), and FKBP65 (FKBP10), due to posttranslational modifications of proline residues in the substrate. PMID: 28385890
  6. FKBP14 expression was elevated in ovarian cancer tissues when compared with matched normal tissues. Lentiviral shRNA mediated knockdown of FKBP14 and suppressed the growth of ovarian cancer cells via arresting the cell cycle in the G0/G1 phase and stimulating cell apoptosis. Moreover, cell apoptosis induced by FKBP14 RNAi was mediated by enhancing the ratio of Bax/Bcl-2. PMID: 27131312
  7. Reduced expression of FKBP14 markedly impaired the proliferative ability of ovarian cancer cells. Additionally, ovarian cancer cells infected with FKBP14 shRNA lentivirus tended to arrest in the G0/G1 phase and undergo apoptosis. PMID: 27931282
  8. the occurrence of umbilical skin redundancy in association with two other syndromes: Morquio syndrome and FKBP14-related Ehlers-Danlos syndrome (EDS), is reported. PMID: 24773188
  9. FKBP22 catalyzes the folding of type III collagen and only interacts with type III type VI and type X collagen. PMID: 24821723
  10. A 1.9 A resolution crystal structure for human FKBP22 has been determined. The EF-hand motifs of two FKBP22 molecules form a dimeric complex with an elongated and predominantly hydrophobic cavity that can potentially be occupied by an aliphatic ligand. PMID: 24272907
  11. study demonstrated FKBP14 is localized in the endoplasmic reticulum (ER) and that deficiency of FKBP14 leads to enlarged ER cisterns in dermal fibroblasts in vivo. PMID: 22265013


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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