FKBP6 293 Cell Lysate Storage: Store at -80°C

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From Biology to Discovery™ FKBP6 293 Cell Lysate Storage: Store at -80°C. Minimize freeze-thaw cycles. After addition of 2X SDS Loading Buffer, the lysates can be stored Subcategory: Cell Lysate at -20°C. Product is guaranteed 6 months from the date of Cat. No.: 408657 shipment. Unit: 0.1 mg For research use only, not for diagnostic or therapeutic Description: procedures. Antigen standard for FK506 binding protein 6, 36kDa (FKBP6), transcript variant 1 is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene- carrying pCMV plasmid (OriGene Technologies, Inc.) and then lysed in RIPA Buffer. Protein concentration was determined using a colorimetric assay. The antigen control carries a C-terminal Myc/DDK tag for detection. Applications: ELISA, WB, IP Format: This product includes 3 vials: 1 vial of gene-specific cell lysate, 1 vial of control vector cell lysate, and 1 vial of loading buffer. Each lysate vial contains 0.1 mg lysate in 0.1 ml (1 mg/ml) of RIPA Buffer (50 mM Tris-HCl pH7.5, 250 mM NaCl, 5 mM EDTA, 50 mM NaF, 1% NP40). The loading buffer vial contains 0.5 ml 2X SDS Loading Buffer (125 mM Tris-Cl, pH6.8, 10% glycerol, 4% SDS, 0.002% Bromophenol blue, 5% beta-mercaptoethanol). Alternate Names: isoform a is encoded by transcript variant 1; FK506-binding protein 6 (36kD); peptidylprolyl cis-trans isomerase; rotamase; immunophilin FKBP36; FKBP-6; FKBP- 36; 36 kDa FKBP; PPIase FKBP6; 36 kDa FK506-binding protein; peptidyl-prolyl cis-trans isomeras; FKBP6; FKBP36; MGC87179; PPIase Accession No.: NP_003593 Application Notes: WB: Mix equal volume of lysates with 2X SDS Loading Buffer. Boil the mixture for 10 min before loading (for membrane protein lysates, incubate the mixture at room temperature for 30 min). Load 5 ug lysate per lane. Abbiotec, LLC • 7985 Dunbrook Rd, Ste A, San Diego, CA 92126 • USA Ph: 858.586.0500 • Fax: 858.586.6252 • Email: [email protected] • www.abbiotec.com.

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Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins
Technical note Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl cis/trans Isomerases (PPIase) Andrzej Galat Retired from: Service d’Ingénierie Moléculaire des Protéines (SIMOPRO), CEA-Université Paris-Saclay, France; [email protected]; Tel.: +33-0164465072 Received: 21 December 2018; Accepted: 21 January 2019; Published: 11 February 2019 Abstract: In this technical note, we describe analyses of more than 15,000 sequences of FK506- binding proteins (FKBP) and cyclophilins, also known as peptidyl-prolyl cis/trans isomerases (PPIases). We have developed a novel way of displaying relative changes of amino acid (AA)- residues at a given sequence position by using heat-maps. This type of representation allows simultaneous estimation of conservation level in a given sequence position in the entire group of functionally-related paralogues (multigene family of proteins). We have also proposed that at least two FKBPs, namely FKBP36, encoded by the Fkbp6 gene and FKBP51, encoded by the Fkbp5 gene, can form dimers bound via a disulfide bridge in the nucleus. This type of dimer may have some crucial function in the regulation of some nuclear complexes at different stages of the cell cycle. Keywords: FKBP; cyclophilin; PPIase; heat-map; immunophilin 1 Introduction About 30 years ago, an exciting adventure began in finding some correlations between pharmacological activities of macrocyclic hydrophobic drugs, namely the cyclic peptide cyclosporine A (CsA), and two macrolides, namely FK506 and rapamycin, which have profound and clinically useful immunosuppressive effects, especially in organ transplantations and in combating some immune disorders.
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Synthesis and Application of Light-Switchable Arylazopyrazole Rapamycin Analogs
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The Immunophilins, Fk506 Binding Protein and Cyclophilin, Are Discretely Localized in the Brain: Relationship to Calcineurin
NeuroscienceVol. 62,NO. 2, pp. 569-580,1994 Elsevier Sctence Ltd Copyright 0 1994 IBRO Pergamon 0306-4522(94)E0182-4 Printed in Great Britain. All rights reserved 0306-4522194 $7.00 + 0.00 THE IMMUNOPHILINS, FK506 BINDING PROTEIN AND CYCLOPHILIN, ARE DISCRETELY LOCALIZED IN THE BRAIN: RELATIONSHIP TO CALCINEURIN T. M. DAWSON,*t J. P. STEINER,* W. E. LYONS,*11 M. FOTUHI,* M. BLUE? and S. H. SNYDER*f§l Departments of *Neuroscience, tNeurology, $Pharmacology and Molecular Sciences, and §Psychiatry, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, U.S.A. (IDivision of Toxicological Science, Johns Hopkins University School of Hygiene and Public Health Abstract-The immunosuppressant drugs cyclosporin A and FK506 bind to small, predominantly soluble proteins cyclophilin and FK506 binding protein, respectively, to mediate their pharmacological actions. The immunosuppressant actions of these drugs occur through binding of cyclophilin-cyclosporinA and FK506 binding protein-FK506 complexes to the calcium-calmodulin-dependent protein phosphatase, calcineurin, inhibiting phosphatase activity, Utilizing immunohistcchemistry, in situ hybridization and autoradiography, we have localized protein and messenger RNA for FKS06 binding protein, cyclophilin and calcineurin. All three proteins and/or messages exhibit a heterogenous distribution through the brain and spinal cord, with the majority of the localizations being neuronal. We observe a striking co-localiz- ation of FK506 binding protein and calcineurin in most
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FKBP Family Proteins: Immunophilins with Versatile Biological Functions
This document is downloaded from DR‑NTU (https://dr.ntu.edu.sg) Nanyang Technological University, Singapore. FKBP family proteins : immunophilins with versatile biological functions Kang, Cong Bao; Ye, Hong; Dhe‑Paganon, Sirano; Yoon, Ho Sup 2008 Kang, C. B., Ye, H., Dhe‑Paganon, S., & Yoon, H. S. (2008). FKBP family proteins : immunophilins with versatile biological functions. Neurosignals, 16(4), 318–325. https://hdl.handle.net/10356/95238 https://doi.org/10.1159/000123041 © 2008 S. Karger AG, Basel. This is the author created version of a work that has been peer reviewed and accepted for publication by Neurosignals, S. Karger AG, Basel. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: http://dx.doi.org/10.1159/000123041. Downloaded on 28 Sep 2021 01:49:48 SGT FKBP Family Proteins: Immunophilins with Versatile Biological Functions Cong Bao Kang a, Hong Ye a, Sirano Dhe-Paganon b, Ho Sup Yoon a,* a School of Biological Science, Nanyang Technological University, Singapore , Singapore; b Structural Genomics Consortium and Physiology, Banting Institute, University of Toronto, Toronto, Ont. , Canada * Tel. +65 6316 2846, Fax +65 6791 3856, E-Mail [email protected] Key Words Immunophilin • FK506-binding protein • Peptidylprolyl cis/trans isomerase • Immunophilin ligand • Neuroprotection • FK506 • Rapamycin Abstract Immunophilins consist of a family of highly conserved proteins binding with immunosuppressive drugs such as FK506, rapamycin and cyclosporin A. FK506-binding protein (FKBP) is one of two major immunophilins and most of FKBP family members bind FK506 and show peptidylprolyl cis/trans isomerase (PPIase) activity.
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R EPORTS tion, we mutated this position in the PGT 24. W. G. Cance, R. J. Craven, T. M. Weiner, E. T. Liu, Int. Foundation and, in part, by a grant from the Israel minigene. As seen in Fig. 4B (lanes 4 and 5), J. Cancer 54, 571 (1993). Cancer Association and the Indian-Israeli Scientiﬁc Research Corporation to G.A. this point mutation was enough to activate the 25. I. W. Caras et al., Nature 325, 545 (1987). 26. G. Svineng, R. Fassler, S. Johansson, Biochem. J. 330, Supporting Online Material nearly constitutive inclusion of the Alu exon 1255 (1998). www.sciencemag.org/cgi/content/full/300/5623/1288/ in the mature transcript. As indicated above, 27. J. Jurka, A. Milosavljevic, J. Mol. Evol. 32, 105(1991). DC1 the same mutation in the COL4A3 gene ac- 28. RepeatMasker is available online at http://repeatmas- Materials and Methods ker.genome.washington.edu/cgi-bin/RepeatMasker. tivates a constitutive exonization of a silent Fig. S1 29. We thank M. Kupiec for a critical reading; R. Reed for Table S1 intronic Alu, resulting in Alport syndrome the hSlu7 plasmid; and also F. Belinky, R. Shalgi, T. References and Notes (10). To assess the importance of our find- Dagan, and E. Sharon for assistance in Alu data analysis. Supported by a grant from the Israel Science 21 January 2003; accepted 9 April 2003 ings, we analyzed the entire content of Alusin the human genome and found that there are at least 238,000 antisense Alus located within introns in the human genome (20).
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