Description
FKBP14 enzyme accelerates the folding of proteins during protein synthesis. It contains 2 EF-hand domains and one PPIase FKBP-type domain. Truncation of the amino-terminus of FKBP14 significantly decreases peptidyl prolyl cis-trans isomerase activity, therefore suggesting that the PPIase FKBP-type domain must be located at the N-terminus.
6354 | Human Recombinant FKBP14 DataSheet
Biomolecule/Target: N/A
Synonyms: Human Recombinant FKBP14
Alternates names: Peptidyl-prolyl cis-trans isomerase FKBP14, FKBP22
Taglines: An immunophilin family protein functioning as a protein folding chaperone
NCBI Gene ID #: 3596
NCBI Gene Symbol: IL13
Gene Source: Human
Accession #: P35225
Recombinant: Yes
Source: E. Coli
Purity by SDS-PAGEs: 98%
Assay: SDS-PAGE
Purity: N/A
Assay #2: N/A
Endotoxin Level: N/A
Activity (Specifications/test method): N/A
Biological activity: Specific activity is > 240 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1 µmole of Suc-AAFP-pNA per minute at 25°C in Tris HCl pH 8.0 using chymotrypsin.
Results: N/A
Binding Capacity: N/A
Unit Definition: Specific activity is defined as the amount of enzyme that cleaves 1 µmole of Suc-AAFP-pNA per minute at 25°C in Tris HCl pH 8.0 using chymotrypsin.
Molecular Weight: 24.2 kDa (213 aa, 20-211 aa + NT His Tag)
Concentration: 1 mg/ml
Appearance: Liquid
Physical form description: 1 mg/ml solution in PBS (pH 7.4) containing 10% glycerol.
Reconstitution Instructions: N/A
Amino acid sequence: MGSSHHHHHH SSGLVPRGSH MALIPEPEVK IEVLQKPFIC HRKTKGGDLM LVHYEGYLEK DGSLFHSTHK HNNGQPIWFT LGILEALKGW DQGLKGMCVG EKRKLIIPPA LGYGKEGKGK IPPESTLIFN IDLLEIRNGP RSHESFQEMD LNDDWKLSKD EVKAYLKKEF EKHGAVVNES HHDALVEDIF DKEDEDKDGF ISAREFTYKH DEL