Peptidyl-prolyl cis-trans isomerase FKBP14 Recombinant Protein | FKBP14 recombinant protein

Recombinant Human Peptidyl-prolyl cis-trans isomerase FKBP14

Cat. Num. AAA1337465

• Gene Names: FKBP14; EDSKMH; FKBP22; IPBP12
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Peptidyl-prolyl cis-trans isomerase FKBP14; Recombinant Human Peptidyl-prolyl cis-trans isomerase FKBP14; 22 kDa FK506-binding protein; 22 kDa FKBP; FKBP-22; FK506-binding protein 14; FKBP-14; Rotamase; FKBP14 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 20-211aa; Full Length
• Sequence: ALIPEPEVKIEVLQKPFICHRKTKGGDLMLVHYEGYLEKDGSLFHSTHKHNNGQPIWFTLGILEALKGWDQGLKGMCVGEKRKLIIPPALGYGKEGKGKIPPESTLIFNIDLLEIRNGPRSHESFQEMDLNDDWKLSKDEVKAYLKKEFEKHGAVVNESHHDALVEDIFDKEDEDKDGFISAREFTYKHDEL
• Sequence Length: 211

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for FKBP14 recombinant protein

PPIases accelerate the folding of proteins during protein synthesis.

References

The secreted protein discovery initiative (SPDI) , a large-scale effort to identify novel human secreted and transmembrane proteins a bioinformatics assessment.Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.Genome Res. 13:2265-2270(2003) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Signal peptide prediction based on analysis of experimentally verified cleavage sites.Zhang Z., Henzel W.J.Protein Sci. 13:2819-2824(2004) Mutations in FKBP14 cause a variant of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss.Baumann M., Giunta C., Krabichler B., Ruschendorf F., Zoppi N., Colombi M., Bittner R.E., Quijano-Roy S., Muntoni F., Cirak S., Schreiber G., Zou Y., Hu Y., Romero N.B., Carlier R.Y., Amberger A., Deutschmann A., Straub V., Rohrbach M., Steinmann B., Rostasy K., Karall D., Bonnemann C.G., Zschocke J., Fauth C.Am. J. Hum. Genet. 90:201-216(2012)

NCBI and Uniprot Product Information

• NCBI GI #: 8923659
• NCBI GeneID: 55033
• NCBI Accession #: NP_060416.1
• NCBI GenBank Nucleotide #: NM_017946.3
• UniProt Accession #: Q9NWM8
• Molecular Weight: 38 kDa
• NCBI Official Full Name: peptidyl-prolyl cis-trans isomerase FKBP14
• NCBI Official Synonym Full Names: FK506 binding protein 14
• NCBI Official Symbol: FKBP14
• NCBI Official Synonym Symbols: EDSKMH; FKBP22; IPBP12
• NCBI Protein Information: peptidyl-prolyl cis-trans isomerase FKBP14
• UniProt Protein Name: Peptidyl-prolyl cis-trans isomerase FKBP14
• Protein Family: Peptidyl-prolyl cis-trans isomerase
• UniProt Gene Name: FKBP14
• UniProt Synonym Gene Names: FKBP22; PPIase FKBP14; 22 kDa FKBP; FKBP-22; FKBP-14
• UniProt Entry Name: FKB14_HUMAN

NCBI Description

The protein encoded by this gene is a member of the FK506-binding protein family of peptidyl-prolyl cis-trans isomerases. The encoded protein is found in the lumen of the endoplasmic reticulum, where it is thought to accelerate protein folding. Defects in this gene are a cause of a type of Ehlers-Danlos syndrome (EDS). Both a protein-coding variant and noncoding variants are transcribed from this gene. [provided by RefSeq, Mar 2012]

Uniprot Description

FKBP14: PPIases accelerate the folding of proteins during protein synthesis. Defects in FKBP14 are the cause of Ehlers-Danlos syndrome with progressive kyphoscoliosis, myopathy, and hearing loss (EDSKMH). 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. Clinically, this disorder is characterized by the following features: severe generalized hypotonia at birth with marked muscle weakness that improve in infancy; early-onset progressive kyphoscoliosis; joint hypermobility without contractures; hyperelastic skin with follicular hyperkeratosis, easy bruising, and occasional abnormal scarring; myopathy as confirmed by muscle MRI, histology, and electron microscopy; hearing impairment, which is predominantly sensorineural; and a normal ratio of lysyl pyridinoline to hydroxylysyl pyridinoline (LP/HP) in urine.

Protein type: Isomerase; EC 5.2.1.8; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 7p14.3

Cellular Component: endoplasmic reticulum lumen; endoplasmic reticulum membrane

Molecular Function: calcium ion binding; FK506 binding; peptidyl-prolyl cis-trans isomerase activity

Biological Process: cellular protein metabolic process; protein peptidyl-prolyl isomerization; unfolded protein response

Disease: Ehlers-danlos Syndrome With Progressive Kyphoscoliosis, Myopathy, And Hearing Loss