Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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)

 FKBP6_HUMAN             Reviewed;         327 AA.
O75344; B4DXT7; G3V0I2; Q7Z4T4; Q9UDS0;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-APR-2018, entry version 166.
RecName: Full=Inactive peptidyl-prolyl cis-trans isomerase FKBP6;
Short=Inactive PPIase FKBP6;
AltName: Full=36 kDa FK506-binding protein;
Short=36 kDa FKBP;
Short=FKBP-36;
AltName: Full=FK506-binding protein 6;
Short=FKBP-6;
AltName: Full=Immunophilin FKBP36;
Name=FKBP6; Synonyms=FKBP36;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=9782077; DOI=10.1006/geno.1998.5412;
Meng X., Lu X., Morris C.A., Keating M.T.;
"A novel human gene FKBP6 is deleted in Williams syndrome.";
Genomics 52:130-137(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Zan Q., Guo J.H., Yu L.;
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
POSSIBLE INVOLVEMENT IN WBS.
PubMed=15770126; DOI=10.1097/00019605-200504000-00002;
Metcalfe K., Simeonov E., Beckett W., Donnai D., Tassabehji M.;
"Autosomal dominant inheritance of Williams-Beuren syndrome in a
father and son with haploinsufficiency for FKBP6.";
Clin. Dysmorphol. 14:61-65(2005).
[8]
VARIANT CYS-183, AND POSSIBLE INVOLVEMENT IN AZOOSPERMIA.
PubMed=16227348; DOI=10.1093/molehr/gah232;
Westerveld G.H., Repping S., Lombardi M.P., van der Veen F.;
"Mutations in the chromosome pairing gene FKBP6 are not a common cause
of non-obstructive azoospermia.";
Mol. Hum. Reprod. 11:673-675(2005).
[9]
POSSIBLE INVOLVEMENT IN AZOOSPERMIA.
PubMed=17307919; DOI=10.1530/REP-06-0125;
Zhang W., Zhang S., Xiao C., Yang Y., Zhoucun A.;
"Mutation screening of the FKBP6 gene and its association study with
spermatogenic impairment in idiopathic infertile men.";
Reproduction 133:511-516(2007).
[10]
INTERACTION WITH HSPA2 AND CLTC.
PubMed=18529014; DOI=10.1021/bi8001506;
Jarczowski F., Fischer G., Edlich F.;
"FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes.";
Biochemistry 47:6946-6952(2008).
[11]
INTERACTION WITH GAPDH.
PubMed=19001379; DOI=10.1074/jbc.M709779200;
Jarczowski F., Jahreis G., Erdmann F., Schierhorn A., Fischer G.,
Edlich F.;
"FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate
dehydrogenase inhibitor.";
J. Biol. Chem. 284:766-773(2009).
-!- FUNCTION: Co-chaperone required during spermatogenesis to repress
transposable elements and prevent their mobilization, which is
essential for the germline integrity. Acts via the piRNA metabolic
process, which mediates the repression of transposable elements
during meiosis by forming complexes composed of piRNAs and Piwi
proteins and govern the methylation and subsequent repression of
transposons. Acts as a co-chaperone via its interaction with HSP90
and is required for the piRNA amplification process, the secondary
piRNA biogenesis. May be required together with HSP90 in removal
of 16 nucleotide ping-pong by-products from Piwi complexes,
possibly facilitating turnover of Piwi complexes (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts (via TPR repeats) with HSP90 (By similarity).
Interacts with HSP72/HSPA2 and CLTC. Interacts with GAPDH; leading
to inhibit GAPDH catalytic activity. {ECO:0000250,
ECO:0000269|PubMed:18529014, ECO:0000269|PubMed:19001379}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-744771, EBI-744771;
G2XKQ0:-; NbExp=8; IntAct=EBI-744771, EBI-10175576;
Q9WMX2:- (xeno); NbExp=6; IntAct=EBI-744771, EBI-6863748;
Q8IYA8:CCDC36; NbExp=6; IntAct=EBI-744771, EBI-8638439;
Q96JB5:CDK5RAP3; NbExp=8; IntAct=EBI-744771, EBI-718818;
Q14318:FKBP8; NbExp=2; IntAct=EBI-744771, EBI-724839;
Q9BRK4:LZTS2; NbExp=6; IntAct=EBI-744771, EBI-741037;
P50222:MEOX2; NbExp=5; IntAct=EBI-744771, EBI-748397;
Q9Y5B8:NME7; NbExp=3; IntAct=EBI-744771, EBI-744782;
P22059:OSBP; NbExp=2; IntAct=EBI-744771, EBI-2681902;
Q3UJD6-2:Usp19 (xeno); NbExp=2; IntAct=EBI-744771, EBI-9359023;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
{ECO:0000250}. Chromosome {ECO:0000250}. Note=Does not localize to
pi-bodies. Localizes to meiotic chromosome cores and regions of
homologous chromosome synapsis (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O75344-1; Sequence=Displayed;
Name=2;
IsoId=O75344-2; Sequence=VSP_042038;
Note=No experimental confirmation available.;
Name=3;
IsoId=O75344-3; Sequence=VSP_054251;
-!- TISSUE SPECIFICITY: Detected in all tissues examined, with higher
expression in testis, heart, skeletal muscle, liver, and kidney.
-!- DISEASE: Note=FKBP6 is located in the Williams-Beuren syndrome
(WBS) critical region. WBS results from a hemizygous deletion of
several genes on chromosome 7q11.23, thought to arise as a
consequence of unequal crossing over between highly homologous
low-copy repeat sequences flanking the deleted region.
Haploinsufficiency of FKBP6 may be the cause of certain
cardiovascular and musculo-skeletal abnormalities observed in the
disease (PubMed:9782077). A father and son with Williams-Beuren
syndrome appear to have a common heterozygous deletion that
includes FKBP6 gene. However, the haploinsufficiency for FKBP6
does not appear to preclude male fertility (PubMed:15770126).
{ECO:0000269|PubMed:15770126, ECO:0000269|PubMed:9782077}.
-!- DISEASE: Note=Defects in FKBP6 may be a cause of azoospermia. A
study based on 323 patients with azoospermia or severe
oligozoospermia suggested an association between FKBP6 variants
and azoospermia (PubMed:17307919). However, other studies suggest
that defects in FKBP6 are not a common cause of non-obstructive
azoospermia (PubMed:16227348). {ECO:0000269|PubMed:16227348,
ECO:0000269|PubMed:17307919}.
-!- SIMILARITY: Belongs to the FKBP6 family. {ECO:0000305}.
-!- CAUTION: Although it contains a PPIase FKBP-type domain, does not
show peptidyl-prolyl cis-trans isomerase activity. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF038847; AAC64249.1; -; mRNA.
EMBL; AF447060; AAP97324.1; -; mRNA.
EMBL; AK302121; BAG63499.1; -; mRNA.
EMBL; BC036817; AAH36817.1; -; mRNA.
EMBL; AC005049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471200; EAW69684.1; -; Genomic_DNA.
EMBL; CH471200; EAW69686.1; -; Genomic_DNA.
CCDS; CCDS43595.1; -. [O75344-1]
CCDS; CCDS47604.1; -. [O75344-2]
CCDS; CCDS64670.1; -. [O75344-3]
RefSeq; NP_001128683.1; NM_001135211.2. [O75344-2]
RefSeq; NP_001268233.1; NM_001281304.1. [O75344-3]
RefSeq; NP_003593.3; NM_003602.4. [O75344-1]
UniGene; Hs.661266; -.
PDB; 3B7X; X-ray; 2.10 A; A=12-144.
PDBsum; 3B7X; -.
ProteinModelPortal; O75344; -.
SMR; O75344; -.
BioGrid; 114046; 38.
IntAct; O75344; 45.
STRING; 9606.ENSP00000252037; -.
iPTMnet; O75344; -.
PhosphoSitePlus; O75344; -.
MaxQB; O75344; -.
PaxDb; O75344; -.
PeptideAtlas; O75344; -.
PRIDE; O75344; -.
DNASU; 8468; -.
Ensembl; ENST00000252037; ENSP00000252037; ENSG00000077800. [O75344-1]
Ensembl; ENST00000413573; ENSP00000394952; ENSG00000077800. [O75344-3]
Ensembl; ENST00000431982; ENSP00000416277; ENSG00000077800. [O75344-2]
GeneID; 8468; -.
KEGG; hsa:8468; -.
UCSC; uc003tya.4; human. [O75344-1]
CTD; 8468; -.
DisGeNET; 8468; -.
EuPathDB; HostDB:ENSG00000077800.11; -.
GeneCards; FKBP6; -.
H-InvDB; HIX0006777; -.
H-InvDB; HIX0078779; -.
H-InvDB; HIX0114828; -.
HGNC; HGNC:3722; FKBP6.
HPA; HPA061109; -.
MIM; 604839; gene.
neXtProt; NX_O75344; -.
OpenTargets; ENSG00000077800; -.
PharmGKB; PA28163; -.
eggNOG; KOG0543; Eukaryota.
eggNOG; COG0545; LUCA.
GeneTree; ENSGT00760000119159; -.
HOGENOM; HOG000251594; -.
HOVERGEN; HBG051625; -.
InParanoid; O75344; -.
KO; K09572; -.
OMA; CPPRIKP; -.
OrthoDB; EOG091G0FWD; -.
PhylomeDB; O75344; -.
TreeFam; TF354214; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
ChiTaRS; FKBP6; human.
EvolutionaryTrace; O75344; -.
GenomeRNAi; 8468; -.
PRO; PR:O75344; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000077800; -.
CleanEx; HS_FKBP6; -.
ExpressionAtlas; O75344; baseline and differential.
Genevisible; O75344; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0000795; C:synaptonemal complex; ISS:UniProtKB.
GO; GO:0005528; F:FK506 binding; IBA:GO_Central.
GO; GO:0051879; F:Hsp90 protein binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; ISS:UniProtKB.
GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase.
GO; GO:0006457; P:protein folding; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR023566; PPIase_FKBP.
InterPro; IPR001179; PPIase_FKBP_dom.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR10516; PTHR10516; 1.
Pfam; PF00254; FKBP_C; 1.
SMART; SM00028; TPR; 3.
SUPFAM; SSF48452; SSF48452; 1.
PROSITE; PS50059; FKBP_PPIASE; 1.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosome; Complete proteome;
Cytoplasm; Differentiation; Meiosis; Nucleus; Polymorphism;
Reference proteome; Repeat; RNA-mediated gene silencing;
Spermatogenesis; TPR repeat; Williams-Beuren syndrome.
CHAIN 1 327 Inactive peptidyl-prolyl cis-trans
isomerase FKBP6.
/FTId=PRO_0000075329.
DOMAIN 54 143 PPIase FKBP-type. {ECO:0000255|PROSITE-
ProRule:PRU00277}.
REPEAT 171 204 TPR 1.
REPEAT 219 252 TPR 2.
REPEAT 253 286 TPR 3.
VAR_SEQ 1 19 MGGSALNQGVLEGDDAPGQ -> MSASSWPQNGMPPS (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042038.
VAR_SEQ 59 88 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_054251.
VARIANT 183 183 R -> C (probable polymorphism;
dbSNP:rs147213094).
{ECO:0000269|PubMed:16227348}.
/FTId=VAR_070840.
CONFLICT 103 103 R -> Q (in Ref. 2; AAP97324).
{ECO:0000305}.
CONFLICT 123 123 C -> S (in Ref. 2; AAP97324).
{ECO:0000305}.
CONFLICT 136 136 E -> K (in Ref. 2; AAP97324).
{ECO:0000305}.
HELIX 21 25 {ECO:0000244|PDB:3B7X}.
TURN 26 28 {ECO:0000244|PDB:3B7X}.
STRAND 30 44 {ECO:0000244|PDB:3B7X}.
STRAND 47 50 {ECO:0000244|PDB:3B7X}.
STRAND 56 64 {ECO:0000244|PDB:3B7X}.
STRAND 72 74 {ECO:0000244|PDB:3B7X}.
HELIX 93 100 {ECO:0000244|PDB:3B7X}.
STRAND 107 112 {ECO:0000244|PDB:3B7X}.
HELIX 114 116 {ECO:0000244|PDB:3B7X}.
TURN 117 121 {ECO:0000244|PDB:3B7X}.
TURN 124 126 {ECO:0000244|PDB:3B7X}.
STRAND 133 143 {ECO:0000244|PDB:3B7X}.
SEQUENCE 327 AA; 37214 MW; C137FA629B676623 CRC64;
MGGSALNQGV LEGDDAPGQS LYERLSQRML DISGDRGVLK DVIREGAGDL VAPDASVLVK
YSGYLEHMDR PFDSNYFRKT PRLMKLGEDI TLWGMELGLL SMRRGELARF LFKPNYAYGT
LGCPPLIPPN TTVLFEIELL DFLDCAESDK FCALSAEQQD QFPLQKVLKV AATEREFGNY
LFRQNRFYDA KVRYKRALLL LRRRSAPPEE QHLVEAAKLP VLLNLSFTYL KLDRPTIALC
YGEQALIIDQ KNAKALFRCG QACLLLTEYQ KARDFLVRAQ KEQPFNHDIN NELKKLASCY
RDYVDKEKEM WHRMFAPCGD GSTAGES


Related products :

Catalog number Product name Quantity
18-003-43761 FK506-binding protein 6 - EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase; PPIase; Rotamase; 36 kDa FK506-binding protein; FKBP-36; Immunophilin FKBP36 Polyclonal 0.1 mg Protein A
20-372-60237 FK506 binding protein 3. 25kDa (FKBP3). mRNA - Mouse monoclonal anti-human FKBP3 antibody; EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase; PPIase; Rotamase; 25 kDa FKBP; FKBP-25; Rapamycin-selective 0.1 mg
26-205 FKBP11 belongs to the FKBP family of peptidyl-prolyl cis_trans isomerases, which catalyze the folding of proline-containing polypeptides. The peptidyl-prolyl isomerase activity of FKBP proteins is inh 0.05 mg
18-271-81040 Peptidylprolyl Isomerase - Chicken Anti Peptidylprolyl Isomerase; EC 5.2.1.8; Peptidyl-prolyl cis-trans isomerase; PPIase; Rotamase; FKBP-21; NcFKBP22 Polyclonal 0.1 mg
OETENZ-338 FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant 20
OETENZ-338 FKBP-Type Peptidyl-Prolyl Cis-Trans Isomerase E.Coli Recombinant 5
CSB-EL008702BO Bovine Peptidyl-prolyl cis-trans isomerase FKBP6(FKBP6) ELISA kit 96T
CSB-EL008702MO Mouse Peptidyl-prolyl cis-trans isomerase FKBP6(FKBP6) ELISA kit 96T
CSB-EL008702HU Human Peptidyl-prolyl cis-trans isomerase FKBP6(FKBP6) ELISA kit 96T
CSB-EL008702BO Bovine Peptidyl-prolyl cis-trans isomerase FKBP6(FKBP6) ELISA kit SpeciesBovine 96T
CSB-EL008702HU Human Peptidyl-prolyl cis-trans isomerase FKBP6(FKBP6) ELISA kit SpeciesHuman 96T
CSB-EL008702MO Mouse Peptidyl-prolyl cis-trans isomerase FKBP6(FKBP6) ELISA kit SpeciesMouse 96T
FKBP6_MOUSE ELISA Kit FOR Peptidyl-prolyl cis-trans isomerase FKBP6; organism: Mouse; gene name: Fkbp6 96T
29-825 FKBP6 is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP6 is a cis-trans prolyl isomeras 0.1 mg
SIH-214-10MG FK506 FKBP inhibitor CAS Number 109581_93_3 10mg
SIH-214-50MG FK506 FKBP inhibitor CAS Number 109581_93_3 50mg
EIAAB32019 40 kDa peptidyl-prolyl cis-trans isomerase,Bos taurus,Bovine,Cyclophilin-40,Cyclophilin-related protein,CYP-40,CYPD,Estrogen receptor-binding cyclophilin,Peptidyl-prolyl cis-trans isomerase D,PPIase D
enz-516 Recombinant Human FK506 Binding Protein 6 FKBP6 10
enz-516 Recombinant Human FK506 Binding Protein 6 FKBP6 2
enz-516 Recombinant Human FK506 Binding Protein 6 FKBP6 1mg
FKBP6 FKBP4 Gene FK506 binding protein 4, 59kDa
FKBP8 FKBP6 Gene FK506 binding protein 6, 36kDa
201-20-2064 FKBP6{FK506 binding protein 6, 36kDa}rabbit.pAb 0.2ml
GWB-C0F1CD Anti- FKBP6 (FK506 binding protein 6. 36kDa) Antibody
FKBP6_MOUSE Mouse ELISA Kit FOR Peptidyl-prolyl cis-trans isomerase FKBP6 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur