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Peptidyl-prolyl cis-trans isomerase FKBP42 (PPIase FKBP42) (EC 5.2.1.8) (42 kDa peptidyl-prolyl isomerase) (FK506-binding protein 42) (AtFKBP42) (Immunophilin FKBP42) (Protein TWISTED DWARF 1) (Protein ULTRACURVATA 2) (Rotamase)

 FKB42_ARATH             Reviewed;         365 AA.
Q9LDC0; Q8RWM0;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
08-MAY-2019, entry version 138.
RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP42;
Short=PPIase FKBP42;
EC=5.2.1.8;
AltName: Full=42 kDa peptidyl-prolyl isomerase;
AltName: Full=FK506-binding protein 42;
Short=AtFKBP42;
AltName: Full=Immunophilin FKBP42;
AltName: Full=Protein TWISTED DWARF 1;
AltName: Full=Protein ULTRACURVATA 2;
AltName: Full=Rotamase;
Name=FKBP42; Synonyms=TWD1, UCU2; OrderedLocusNames=At3g21640;
ORFNames=MIL23.21;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Kolukisaoglu U., Berger J., Eckhoff A., Moeller A., Saal B.,
Bellini C., Schulz B.;
"Structure and evolution of FKBP-like genes in Arabidopsis.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10819329; DOI=10.1093/dnares/7.2.131;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
features of the regions of 4,504,864 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:131-135(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
SUBCELLULAR LOCATION, INTERACTION WITH CALMODULIN AND SHD/HSP90, AND
DISRUPTION PHENOTYPE.
PubMed=12410806; DOI=10.1046/j.1365-313X.2002.01420.x;
Kamphausen T., Fanghaenel J., Neumann D., Schulz B., Rahfeld J.-U.;
"Characterization of Arabidopsis thaliana AtFKBP42 that is membrane-
bound and interacts with Hsp90.";
Plant J. 32:263-276(2002).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MDR1/PGP1 AND
MDR11/PGP19.
PubMed=14517332; DOI=10.1091/mbc.E02-10-0698;
Geisler M., Kolukisaoglu H.U., Bouchard R., Billion K., Berger J.,
Saal B., Frangne N., Koncz-Kalman Z., Koncz C., Dudler R.,
Blakeslee J.J., Murphy A.S., Martinoia E., Schulz B.;
"TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like
protein, interacts with Arabidopsis multidrug resistance-like
transporters AtPGP1 and AtPGP19.";
Mol. Biol. Cell 14:4238-4249(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MRP1 AND MRP2.
PubMed=15133126; DOI=10.1091/mbc.E03-11-0831;
Geisler M., Girin M., Brandt S., Vincenzetti V., Plaza S., Paris N.,
Kobae Y., Maeshima M., Billion K., Kolukisaoglu U.H., Schulz B.,
Martinoia E.;
"Arabidopsis immunophilin-like TWD1 functionally interacts with
vacuolar ABC transporters.";
Mol. Biol. Cell 15:3393-3405(2004).
[8]
FUNCTION.
PubMed=14730066; DOI=10.1104/pp.103.032524;
Perez-Perez J.M., Ponce M.R., Micol J.L.;
"The ULTRACURVATA2 gene of Arabidopsis encodes an FK506-binding
protein involved in auxin and brassinosteroid signaling.";
Plant Physiol. 134:101-117(2004).
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15047905; DOI=10.1104/pp.103.031005;
He Z., Li L., Luan S.;
"Immunophilins and parvulins. Superfamily of peptidyl prolyl
isomerases in Arabidopsis.";
Plant Physiol. 134:1248-1267(2004).
[10]
FUNCTION.
PubMed=16887800; DOI=10.1074/jbc.M604604200;
Bouchard R., Bailly A., Blakeslee J.J., Oehring S.C., Vincenzetti V.,
Lee O.R., Paponov I., Palme K., Mancuso S., Murphy A.S., Schulz B.,
Geisler M.;
"Immunophilin-like TWISTED DWARF1 modulates auxin efflux activities of
Arabidopsis P-glycoproteins.";
J. Biol. Chem. 281:30603-30612(2006).
[11]
FUNCTION, AND INTERACTION WITH NPA.
PubMed=18499676; DOI=10.1074/jbc.M709655200;
Bailly A., Sovero V., Vincenzetti V., Santelia D., Bartnik D.,
Koenig B.W., Mancuso S., Martinoia E., Geisler M.;
"Modulation of P-glycoproteins by auxin transport inhibitors is
mediated by interaction with immunophilins.";
J. Biol. Chem. 283:21817-21826(2008).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20971896; DOI=10.1105/tpc.110.078360;
Wu G., Otegui M.S., Spalding E.P.;
"The ER-localized TWD1 immunophilin is necessary for localization of
multidrug resistance-like proteins required for polar auxin transport
in Arabidopsis roots.";
Plant Cell 22:3295-3304(2010).
[13]
X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 1-180.
PubMed=16364310; DOI=10.1016/j.febslet.2005.12.007;
Weiergraeber O.H., Eckhoff A., Granzin J.;
"Crystal structure of a plant immunophilin domain involved in
regulation of MDR-type ABC transporters.";
FEBS Lett. 580:251-255(2006).
[14]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-338.
PubMed=17045295; DOI=10.1016/j.jmb.2006.09.052;
Granzin J., Eckhoff A., Weiergraber O.H.;
"Crystal structure of a multi-domain immunophilin from Arabidopsis
thaliana: a paradigm for regulation of plant ABC transporters.";
J. Mol. Biol. 364:799-809(2006).
[15]
STRUCTURE BY NMR OF 335-365, AND MEMBRANE ANCHOR.
PubMed=17033777; DOI=10.1007/s00249-006-0094-2;
Scheidt H.A., Vogel A., Eckhoff A., Koenig B.W., Huster D.;
"Solid-state NMR characterization of the putative membrane anchor of
TWD1 from Arabidopsis thaliana.";
Eur. Biophys. J. 36:393-404(2007).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides (By similarity). Modulates the uptake of MRP
substrates into the vacuole; reduces metolachlor-GS (MOC-GS) and
enhances 17-beta-estradiol 17-(beta-D-glucuronide) (E(2)17betaG)
uptake. Regulates cell elongation and orientation. Functions as a
positive regulator of PGP1-mediated auxin transport. Confers drug
modulation of PGP1 efflux activity as interaction with NPA or
flavonol quercetin prevents its physical and functional
interaction with PGP1. Required for the proper localization of
auxin-related ABCB transporters. Plays a role in brassinosteroid
(BR) signaling pathway. {ECO:0000250, ECO:0000269|PubMed:14517332,
ECO:0000269|PubMed:14730066, ECO:0000269|PubMed:15133126,
ECO:0000269|PubMed:16887800, ECO:0000269|PubMed:18499676,
ECO:0000269|PubMed:20971896}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-peptidylproline (omega=180) = [protein]-
peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
ChEBI:CHEBI:83834; EC=5.2.1.8;
-!- SUBUNIT: Interacts with calmodulin (CaM), MRP1, MRP2, MDR1/PGP1,
MDR11/PGP19 and SHD/HSP90. Interacts with 1-naphthylphthalamic
acid (NPA). {ECO:0000269|PubMed:12410806,
ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:15133126,
ECO:0000269|PubMed:18499676}.
-!- INTERACTION:
Q9ZR72:ABCB1; NbExp=2; IntAct=EBI-360006, EBI-366396;
Q9C8G9:ABCC1; NbExp=4; IntAct=EBI-360006, EBI-637633;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12410806,
ECO:0000269|PubMed:14517332, ECO:0000269|PubMed:15133126}; Single-
pass type IV membrane protein. Vacuole membrane
{ECO:0000269|PubMed:12410806, ECO:0000269|PubMed:15133126};
Single-pass type IV membrane protein. Endoplasmic reticulum
{ECO:0000269|PubMed:20971896}.
-!- DISRUPTION PHENOTYPE: Plants display helical rotation of several
organs. {ECO:0000269|PubMed:12410806}.
-!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ224640; CAC00654.1; -; mRNA.
EMBL; AB019232; BAB02359.1; -; Genomic_DNA.
EMBL; CP002686; AEE76533.1; -; Genomic_DNA.
EMBL; AY093009; AAM13008.1; -; mRNA.
EMBL; BT001192; AAN65079.1; -; mRNA.
RefSeq; NP_188801.2; NM_113059.3.
PDB; 2F4E; X-ray; 2.32 A; A/B=1-180.
PDB; 2IF4; X-ray; 2.85 A; A=1-338.
PDBsum; 2F4E; -.
PDBsum; 2IF4; -.
SMR; Q9LDC0; -.
BioGrid; 7050; 31.
IntAct; Q9LDC0; 26.
STRING; 3702.AT3G21640.1; -.
TCDB; 8.A.11.1.1; the immunophilin-like prolyl:peptidyl isomerase regulator (i-ppi) family.
PaxDb; Q9LDC0; -.
PRIDE; Q9LDC0; -.
EnsemblPlants; AT3G21640.1; AT3G21640.1; AT3G21640.
GeneID; 821718; -.
Gramene; AT3G21640.1; AT3G21640.1; AT3G21640.
KEGG; ath:AT3G21640; -.
Araport; AT3G21640; -.
TAIR; locus:2089890; AT3G21640.
eggNOG; KOG0543; Eukaryota.
eggNOG; COG0545; LUCA.
HOGENOM; HOG000006189; -.
InParanoid; Q9LDC0; -.
OMA; NLAMTQI; -.
OrthoDB; 897391at2759; -.
PhylomeDB; Q9LDC0; -.
EvolutionaryTrace; Q9LDC0; -.
PRO; PR:Q9LDC0; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LDC0; baseline and differential.
Genevisible; Q9LDC0; AT.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:TAIR.
GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0048366; P:leaf development; IMP:TAIR.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR039663; AIP/AIPL1.
InterPro; IPR001179; PPIase_FKBP_dom.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR11242; PTHR11242; 1.
Pfam; PF00254; FKBP_C; 1.
Pfam; PF13181; TPR_8; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
PROSITE; PS50005; TPR; 2.
PROSITE; PS50293; TPR_REGION; 2.
1: Evidence at protein level;
3D-structure; Auxin signaling pathway; Calmodulin-binding;
Cell membrane; Complete proteome; Endoplasmic reticulum; Isomerase;
Membrane; Reference proteome; Repeat; Rotamase; TPR repeat;
Transmembrane; Transmembrane helix; Vacuole.
CHAIN 1 365 Peptidyl-prolyl cis-trans isomerase
FKBP42.
/FTId=PRO_0000226087.
TRANSMEM 339 357 Helical; Anchor for type IV membrane
protein.
DOMAIN 67 159 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
REPEAT 179 212 TPR 1.
REPEAT 230 263 TPR 2.
REPEAT 264 297 TPR 3.
REGION 1 163 Interaction with MDR1/PGP1.
REGION 163 337 Interaction with MRP1.
{ECO:0000269|PubMed:15133126}.
REGION 310 326 Calmodulin-binding. {ECO:0000255}.
CONFLICT 107 107 A -> P (in Ref. 4; AAM13008/AAN65079).
{ECO:0000305}.
STRAND 45 48 {ECO:0000244|PDB:2F4E}.
STRAND 51 57 {ECO:0000244|PDB:2F4E}.
STRAND 69 78 {ECO:0000244|PDB:2F4E}.
TURN 79 81 {ECO:0000244|PDB:2F4E}.
STRAND 84 87 {ECO:0000244|PDB:2F4E}.
TURN 88 92 {ECO:0000244|PDB:2F4E}.
STRAND 95 98 {ECO:0000244|PDB:2F4E}.
HELIX 104 106 {ECO:0000244|PDB:2F4E}.
HELIX 107 113 {ECO:0000244|PDB:2F4E}.
STRAND 121 126 {ECO:0000244|PDB:2F4E}.
HELIX 128 130 {ECO:0000244|PDB:2F4E}.
TURN 131 135 {ECO:0000244|PDB:2F4E}.
STRAND 137 141 {ECO:0000244|PDB:2F4E}.
STRAND 149 159 {ECO:0000244|PDB:2F4E}.
TURN 166 168 {ECO:0000244|PDB:2IF4}.
HELIX 172 188 {ECO:0000244|PDB:2IF4}.
STRAND 191 193 {ECO:0000244|PDB:2IF4}.
HELIX 196 208 {ECO:0000244|PDB:2IF4}.
HELIX 211 215 {ECO:0000244|PDB:2IF4}.
HELIX 219 229 {ECO:0000244|PDB:2IF4}.
HELIX 231 241 {ECO:0000244|PDB:2IF4}.
TURN 242 244 {ECO:0000244|PDB:2IF4}.
HELIX 247 259 {ECO:0000244|PDB:2IF4}.
HELIX 264 275 {ECO:0000244|PDB:2IF4}.
TURN 276 278 {ECO:0000244|PDB:2IF4}.
HELIX 280 289 {ECO:0000244|PDB:2IF4}.
SEQUENCE 365 AA; 41806 MW; C939B75EEC79EA87 CRC64;
MDESLEHQTQ THDQESEIVT EGSAVVHSEP SQEGNVPPKV DSEAEVLDEK VSKQIIKEGH
GSKPSKYSTC FLHYRAWTKN SQHKFEDTWH EQQPIELVLG KEKKELAGLA IGVASMKSGE
RALVHVGWEL AYGKEGNFSF PNVPPMADLL YEVEVIGFDE TKEGKARSDM TVEERIGAAD
RRKMDGNSLF KEEKLEEAMQ QYEMAIAYMG DDFMFQLYGK YQDMALAVKN PCHLNIAACL
IKLKRYDEAI GHCNIVLTEE EKNPKALFRR GKAKAELGQM DSARDDFRKA QKYAPDDKAI
RRELRALAEQ EKALYQKQKE MYKGIFKGKD EGGAKSKSLF WLIVLWQWFV SLFSRIFRRH
RVKAD


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Pathways :
WP1493: Carbon assimilation C4 pathway
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1502: Mitochondrial biogenesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism

Related Genes :
[FKBP42 TWD1 UCU2 At3g21640 MIL23.21] Peptidyl-prolyl cis-trans isomerase FKBP42 (PPIase FKBP42) (EC 5.2.1.8) (42 kDa peptidyl-prolyl isomerase) (FK506-binding protein 42) (AtFKBP42) (Immunophilin FKBP42) (Protein TWISTED DWARF 1) (Protein ULTRACURVATA 2) (Rotamase)
[FKBP4 FKBP52] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (51 kDa FK506-binding protein) (FKBP51) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[FKBP4 P59] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[Fkbp4 Fkpb52] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[Fkbp4 Fkbp52] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[FKBP1A FKBP1] Peptidyl-prolyl cis-trans isomerase FKBP1A (PPIase FKBP1A) (EC 5.2.1.8) (12 kDa FK506-binding protein) (12 kDa FKBP) (FKBP-12) (Calstabin-1) (FK506-binding protein 1A) (FKBP-1A) (Immunophilin FKBP12) (Rotamase)
[Fkbp10 Fkbp-rs Fkbp1-rs Fkbp6 Fkbp65 Fkbprp] Peptidyl-prolyl cis-trans isomerase FKBP10 (PPIase FKBP10) (EC 5.2.1.8) (65 kDa FK506-binding protein) (65 kDa FKBP) (FKBP-65) (FK506-binding protein 10) (FKBP-10) (Immunophilin FKBP65) (Rotamase)
[FKBP10 FKBP65 PSEC0056] Peptidyl-prolyl cis-trans isomerase FKBP10 (PPIase FKBP10) (EC 5.2.1.8) (65 kDa FK506-binding protein) (65 kDa FKBP) (FKBP-65) (FK506-binding protein 10) (FKBP-10) (Immunophilin FKBP65) (Rotamase)
[Fkbp8 Fkbp38 Sam11] Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (38 kDa FK506-binding protein) (38 kDa FKBP) (FKBP-38) (mFKBP38) (FK506-binding protein 8) (FKBP-8) (FKBPR38) (Rotamase)
[FKBP4] Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (FK506-binding protein 4) (FKBP-4) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed]
[FKBP8 FKBP38] Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (38 kDa FK506-binding protein) (38 kDa FKBP) (FKBP-38) (hFKBP38) (FK506-binding protein 8) (FKBP-8) (FKBPR38) (Rotamase)
[FPR3 NPI46 YML074C] FK506-binding nuclear protein (EC 5.2.1.8) (FKBP-70) (Nucleolar proline isomerase) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Proline rotamase)
[FK506-bp1 FKBP39 CG6226] 39 kDa FK506-binding nuclear protein (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase)
[FKBP6 FKBP36] Inactive peptidyl-prolyl cis-trans isomerase FKBP6 (Inactive PPIase FKBP6) (36 kDa FK506-binding protein) (36 kDa FKBP) (FKBP-36) (FK506-binding protein 6) (FKBP-6) (Immunophilin FKBP36)
[Ppid] Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (40 kDa peptidyl-prolyl cis-trans isomerase) (Cyclophilin-40) (CYP-40) (Rotamase D)
[PPID CYPD] Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (40 kDa peptidyl-prolyl cis-trans isomerase) (Cyclophilin-40) (CYP-40) (Cyclophilin-related protein) (Estrogen receptor-binding cyclophilin) (Rotamase D)
[slyD b3349 JW3311] FKBP-type peptidyl-prolyl cis-trans isomerase SlyD (PPIase) (EC 5.2.1.8) (Histidine-rich protein) (Metallochaperone SlyD) (Rotamase) (Sensitivity to lysis protein D) (WHP)
[PPID CYP40 CYPD] Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (40 kDa peptidyl-prolyl cis-trans isomerase) (Cyclophilin-40) (CYP-40) (Cyclophilin-related protein) (Rotamase D)
[FKBP59 CG4535] FK506-binding protein 59 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rotamase) (dFKBP59)
[Fkbp8] Peptidyl-prolyl cis-trans isomerase FKBP8 (PPIase FKBP8) (EC 5.2.1.8) (FK506-binding protein 8) (FKBP-8) (Rotamase)
[Fkbp7 Fkbp23] Peptidyl-prolyl cis-trans isomerase FKBP7 (PPIase FKBP7) (EC 5.2.1.8) (23 kDa FK506-binding protein) (23 kDa FKBP) (FKBP-23) (FK506-binding protein 7) (FKBP-7) (Rotamase)
[Ppid] Peptidyl-prolyl cis-trans isomerase D (PPIase D) (EC 5.2.1.8) (40 kDa peptidyl-prolyl cis-trans isomerase) (Cyclophilin-40) (CYP-40) (Rotamase D)
[CYP20-3 ROC4 At3g62030 F21F14.200] Peptidyl-prolyl cis-trans isomerase CYP20-3, chloroplastic (PPIase CYP20-3) (EC 5.2.1.8) (Cyclophilin of 20 kDa 3) (Cyclosporin A-binding protein) (Rotamase CYP20-3) (Rotamase cyclophilin-4)
[PNSL5 CYP20-2 At5g13120 T19L5_80] Photosynthetic NDH subunit of lumenal location 5, chloroplastic (Cyclophilin of 20 kDa 2) (Peptidyl-prolyl cis-trans isomerase CYP20-2) (PPIase CYP20-2) (EC 5.2.1.8) (Rotamase CYP20-2) (Thylakoid lumen PPIase of 20 kDa) (TLP20)
[RRD1 NCS1 YPA1 YIL153W] Serine/threonine-protein phosphatase 2A activator 1 (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase PTPA-1) (PPIase PTPA-1) (Rotamase PTPA-1) (Phosphotyrosyl phosphatase activator 1)
[ESS1 PIN1 PTF1 YJR017C J1452] Peptidyl-prolyl cis-trans isomerase ESS1 (PPIase ESS1) (EC 5.2.1.8) (Parvulin ESS1) (Processing/termination factor 1)
[PIN1 TA18945] Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (TaPIN1) (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase Pin1) (PPIase Pin1) (Rotamase Pin1)
[cyn-4 cyp-4 mog-6 F59E10.2] Peptidyl-prolyl cis-trans isomerase 4 (PPIase 4) (EC 2.3.2.27) (EC 5.2.1.8) (Cyclophilin mog-6) (Cyclophilin-4) (Masculinization of germline protein 6) (RING-type E3 ubiquitin transferase isomerase 4) (Rotamase 4)
[PPIB CYPB] Peptidyl-prolyl cis-trans isomerase B (PPIase B) (EC 5.2.1.8) (CYP-S1) (Cyclophilin B) (Rotamase B) (S-cyclophilin) (SCYLP)
[PPIF CYP3] Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Mitochondrial cyclophilin) (CyP-M) (Rotamase F)

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