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

Autophagy protein 5 (APG5-like)

 ATG5_MOUSE              Reviewed;         275 AA.
Q99J83;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-MAR-2018, entry version 139.
RecName: Full=Autophagy protein 5;
AltName: Full=APG5-like;
Name=Atg5; Synonyms=Apg5l;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CONJUGATION TO ATG12, AND
MUTAGENESIS OF LYS-130.
TISSUE=Embryonic stem cell;
PubMed=11266458; DOI=10.1083/jcb.152.4.657;
Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y.,
Suzuki K., Tokuhisa T., Ohsumi Y., Yoshimori T.;
"Dissection of autophagosome formation using Apg5-deficient mouse
embryonic stem cells.";
J. Cell Biol. 152:657-668(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
INTERACTION WITH ATG10, AND CONJUGATION TO ATG12.
PubMed=12482611; DOI=10.1016/S0014-5793(02)03739-0;
Mizushima N., Yoshimori T., Ohsumi Y.;
"Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the
conjugation-mediated yeast two-hybrid method.";
FEBS Lett. 532:450-454(2002).
[5]
CONJUGATION TO ATG12 BY ATG10, AND FUNCTION.
PubMed=12890687; DOI=10.1074/jbc.M300550200;
Nemoto T., Tanida I., Tanida-Miyake E., Minematsu-Ikeguchi N.,
Yokota M., Ohsumi M., Ueno T., Kominami E.;
"The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation,
facilitates MAP-LC3 modification.";
J. Biol. Chem. 278:39517-39526(2003).
[6]
IDENTIFICATION IN A COMPLEX WITH ATG12 AND ATG16L.
PubMed=12665549; DOI=10.1242/jcs.00381;
Mizushima N., Kuma A., Kobayashi Y., Yamamoto A., Matsubae M.,
Takao T., Natsume T., Ohsumi Y., Yoshimori T.;
"Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic
isolation membrane with the Apg12-Apg5 conjugate.";
J. Cell Sci. 116:1679-1688(2003).
[7]
FUNCTION.
PubMed=17912025; DOI=10.4161/auto.4964;
Nishiyama J., Miura E., Mizushima N., Watanabe M., Yuzaki M.;
"Aberrant membranes and double-membrane structures accumulate in the
axons of Atg5-null Purkinje cells before neuronal death.";
Autophagy 3:591-596(2007).
[8]
FUNCTION.
PubMed=17190837; DOI=10.1084/jem.20061303;
Pua H.H., Dzhagalov I., Chuck M., Mizushima N., He Y.W.;
"A critical role for the autophagy gene Atg5 in T cell survival and
proliferation.";
J. Exp. Med. 204:25-31(2007).
[9]
FUNCTION IN VIRAL INFECTION.
PubMed=17709747; DOI=10.1073/pnas.0704014104;
Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A.,
Xin K.Q., Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.;
"The Atg5-Atg12 conjugate associates with innate antiviral immune
responses.";
Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007).
[10]
FUNCTION.
PubMed=18188005; DOI=10.4161/auto.5474;
Miller B.C., Zhao Z., Stephenson L.M., Cadwell K., Pua H.H., Lee H.K.,
Mizushima N.N., Iwasaki A., He Y.W., Swat W., Virgin H.W.;
"The autophagy gene ATG5 plays an essential role in B lymphocyte
development.";
Autophagy 4:309-314(2008).
[11]
CONJUGATION TO ATG12.
PubMed=18768753; DOI=10.1091/mbc.E08-03-0309;
Sou Y.S., Waguri S., Iwata J., Ueno T., Fujimura T., Hara T.,
Sawada N., Yamada A., Mizushima N., Uchiyama Y., Kominami E.,
Tanaka K., Komatsu M.;
"The Atg8 conjugation system is indispensable for proper development
of autophagic isolation membranes in mice.";
Mol. Biol. Cell 19:4762-4775(2008).
[12]
CONJUGATION TO ATG12.
PubMed=19417210; DOI=10.1182/blood-2008-04-151639;
Zhang J., Randall M.S., Loyd M.R., Dorsey F.C., Kundu M.,
Cleveland J.L., Ney P.A.;
"Mitochondrial clearance is regulated by Atg7-dependent and
-independent mechanisms during reticulocyte maturation.";
Blood 114:157-164(2009).
[13]
FUNCTION.
PubMed=19844159; DOI=10.4161/auto.5.8.9991;
Baerga R., Zhang Y., Chen P.H., Goldman S., Jin S.;
"Targeted deletion of autophagy-related 5 (atg5) impairs adipogenesis
in a cellular model and in mice.";
Autophagy 5:1118-1130(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
FUNCTION.
PubMed=20171125; DOI=10.1016/j.immuni.2009.12.006;
Lee H.K., Mattei L.M., Steinberg B.E., Alberts P., Lee Y.H.,
Chervonsky A., Mizushima N., Grinstein S., Iwasaki A.;
"In vivo requirement for Atg5 in antigen presentation by dendritic
cells.";
Immunity 32:227-239(2010).
[16]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=24089209; DOI=10.1038/nature12639;
Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A.,
Beau I., Codogno P., Satir B.H., Satir P., Cuervo A.M.;
"Functional interaction between autophagy and ciliogenesis.";
Nature 502:194-200(2013).
[17]
FUNCTION.
PubMed=24089205; DOI=10.1038/nature12606;
Tang Z., Lin M.G., Stowe T.R., Chen S., Zhu M., Stearns T., Franco B.,
Zhong Q.;
"Autophagy promotes primary ciliogenesis by removing OFD1 from
centriolar satellites.";
Nature 502:254-257(2013).
-!- FUNCTION: Involved in autophagic vesicle formation. Conjugation
with ATG12, through a ubiquitin-like conjugating system involving
ATG7 as an E1-like activating enzyme and ATG10 as an E2-like
conjugating enzyme, is essential for its function. The ATG12-ATG5
conjugate acts as an E3-like enzyme which is required for
lipidation of ATG8 family proteins and their association to the
vesicle membranes. Involved in mitochondrial quality control after
oxidative damage, and in subsequent cellular longevity. Plays a
critical role in multiple aspects of lymphocyte development and is
essential for both B and T lymphocyte survival and proliferation.
Required for optimal processing and presentation of antigens for
MHC II. Involved in the maintenance of axon morphology and
membrane structures, as well as in normal adipocyte
differentiation. Promotes primary ciliogenesis through removal of
OFD1 from centriolar satellites and degradation of IFT20 via the
autophagic pathway. {ECO:0000269|PubMed:11266458,
ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:17190837,
ECO:0000269|PubMed:17912025, ECO:0000269|PubMed:18188005,
ECO:0000269|PubMed:19844159, ECO:0000269|PubMed:20171125,
ECO:0000269|PubMed:24089205, ECO:0000269|PubMed:24089209}.
-!- FUNCTION: May play an important role in the apoptotic process,
possibly within the modified cytoskeleton. Its expression is a
relatively late event in the apoptotic process, occurring
downstream of caspase activity. Plays a crucial role in IFN-gamma-
induced autophagic cell death by interacting with FADD (By
similarity). {ECO:0000250|UniProtKB:Q9H1Y0}.
-!- FUNCTION: (Microbial infection) May act as a proviral factor. In
association with ATG12, negatively regulates the innate antiviral
immune response by impairing the type I IFN production pathway
upon vesicular stomatitis virus (VSV) infection.
{ECO:0000269|PubMed:17709747}.
-!- SUBUNIT: Forms a conjugate with ATG12 (PubMed:11266458,
PubMed:12890687, PubMed:12665549, PubMed:18768753,
PubMed:19417210). The ATG5-ATG12 conjugate forms a complex with
several units of ATG16L (PubMed:12665549). Interacts with TECPR1;
the interaction is direct and does not take place when ATG16L is
associated with the ATG5-ATG12 conjugate (By similarity).
Interacts with DHX58/RIG-1, IFIH1/MDA5 and MAVS/IPS-1 in monomeric
form as well as in ATG12-ATG5 conjugate form. The interaction with
MAVS is further enhanced upon vesicular stomatitis virus (VSV)
infection (PubMed:17709747). Interacts with ATG3 (By similarity).
Interacts with ATG7 and ATG10 (PubMed:12482611). Interacts with
FADD (By similarity). {ECO:0000250|UniProtKB:Q9H1Y0,
ECO:0000269|PubMed:11266458, ECO:0000269|PubMed:12482611,
ECO:0000269|PubMed:12665549, ECO:0000269|PubMed:12890687,
ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:18768753,
ECO:0000269|PubMed:19417210}.
-!- INTERACTION:
Q9CQY1:Atg12; NbExp=4; IntAct=EBI-2911848, EBI-2911788;
Q8C0J2:Atg16l1; NbExp=4; IntAct=EBI-2911848, EBI-769195;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24089209}.
Preautophagosomal structure membrane
{ECO:0000269|PubMed:24089209}; Peripheral membrane protein
{ECO:0000269|PubMed:24089209}. Note=The conjugate detaches from
the membrane immediately before or after autophagosome formation
is completed. Localizes also to discrete punctae along the ciliary
axoneme and to the base of the ciliary axoneme.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: Conjugated to ATG12; which is essential for autophagy, but is
not required for association with isolation membrane.
-!- PTM: Acetylated by EP300. {ECO:0000250}.
-!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB048349; BAB33383.1; -; mRNA.
EMBL; AK028315; BAC25874.1; -; mRNA.
EMBL; BC002166; AAH02166.1; -; mRNA.
CCDS; CCDS23824.1; -.
RefSeq; NP_001300942.1; NM_001314013.1.
RefSeq; NP_444299.1; NM_053069.6.
RefSeq; XP_011241410.1; XM_011243108.2.
UniGene; Mm.22264; -.
ProteinModelPortal; Q99J83; -.
SMR; Q99J83; -.
BioGrid; 198146; 7.
CORUM; Q99J83; -.
DIP; DIP-46420N; -.
IntAct; Q99J83; 13.
MINT; Q99J83; -.
STRING; 10090.ENSMUSP00000044769; -.
iPTMnet; Q99J83; -.
PhosphoSitePlus; Q99J83; -.
EPD; Q99J83; -.
MaxQB; Q99J83; -.
PaxDb; Q99J83; -.
PeptideAtlas; Q99J83; -.
PRIDE; Q99J83; -.
DNASU; 11793; -.
Ensembl; ENSMUST00000039286; ENSMUSP00000044769; ENSMUSG00000038160.
GeneID; 11793; -.
KEGG; mmu:11793; -.
UCSC; uc007ezt.1; mouse.
CTD; 9474; -.
MGI; MGI:1277186; Atg5.
eggNOG; KOG2976; Eukaryota.
eggNOG; ENOG410XQ71; LUCA.
GeneTree; ENSGT00390000004766; -.
HOGENOM; HOG000007893; -.
HOVERGEN; HBG018731; -.
InParanoid; Q99J83; -.
KO; K08339; -.
OMA; WHYPIGV; -.
OrthoDB; EOG091G0JU7; -.
PhylomeDB; Q99J83; -.
TreeFam; TF314415; -.
Reactome; R-MMU-1632852; Macroautophagy.
Reactome; R-MMU-5205685; Pink/Parkin Mediated Mitophagy.
Reactome; R-MMU-8934903; Receptor Mediated Mitophagy.
PRO; PR:Q99J83; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000038160; -.
CleanEx; MM_ATG5; -.
Genevisible; Q99J83; MM.
GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
GO; GO:0005776; C:autophagosome; IDA:MGI.
GO; GO:0005930; C:axoneme; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0044233; C:ER-mitochondrion membrane contact site; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
GO; GO:0035973; P:aggrephagy; IMP:ParkinsonsUK-UCL.
GO; GO:0019883; P:antigen processing and presentation of endogenous antigen; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:UniProtKB.
GO; GO:0075044; P:autophagy of host cells involved in interaction with symbiont; ISO:MGI.
GO; GO:0000422; P:autophagy of mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
GO; GO:0019725; P:cellular homeostasis; IMP:MGI.
GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
GO; GO:0071500; P:cellular response to nitrosative stress; IMP:ParkinsonsUK-UCL.
GO; GO:0009267; P:cellular response to starvation; IMP:MGI.
GO; GO:0060047; P:heart contraction; IMP:MGI.
GO; GO:0016236; P:macroautophagy; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; IMP:MGI.
GO; GO:0050765; P:negative regulation of phagocytosis; IMP:MGI.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:MGI.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0039689; P:negative stranded viral RNA replication; IMP:MGI.
GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
GO; GO:0048840; P:otolith development; IMP:MGI.
GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
GO; GO:0043687; P:post-translational protein modification; IDA:UniProtKB.
GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; IMP:MGI.
GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
GO; GO:0002739; P:regulation of cytokine secretion involved in immune response; IMP:MGI.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:MGI.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
GO; GO:0042493; P:response to drug; IMP:MGI.
GO; GO:0009620; P:response to fungus; IMP:MGI.
GO; GO:0042311; P:vasodilation; IMP:MGI.
GO; GO:0055015; P:ventricular cardiac muscle cell development; IMP:MGI.
InterPro; IPR007239; Atg5.
PANTHER; PTHR13040; PTHR13040; 1.
Pfam; PF04106; APG5; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Autophagy; Complete proteome; Cytoplasm;
Immunity; Isopeptide bond; Membrane; Reference proteome;
Ubl conjugation.
CHAIN 1 275 Autophagy protein 5.
/FTId=PRO_0000218995.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9H1Y0}.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ATG12).
{ECO:0000250}.
MUTAGEN 130 130 K->R: Loss of conjugation.
{ECO:0000269|PubMed:11266458}.
SEQUENCE 275 AA; 32402 MW; F3FCE652D627B694 CRC64;
MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLP RVSYLTLVTD KVKKHFQKVM
RQEDVSEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNI TVHFKSFPEK DLLHCPSKDA
VEAHFMSCMK EADALKHKSQ VINEMQKKDH KQLWMGLQND RFDQFWAINR KLMEYPPEEN
GFRYIPFRIY QTTTERPFIQ KLFRPVAADG QLHTLGDLLR EVCPSAVAPE DGEKRSQVMI
HGIEPMLETP LQWLSEHLSY PDNFLHISIV PQPTD


Related products :

Catalog number Product name Quantity
orb80926 Human Autophagy Related 5 protein Autophagy Protein Human Recombinant produced in E.coli is non-glycosylated, polypeptide chain having molecular weight of 31.6 kDa. APG5 contains T7 tag at N-terminus 2
15-288-22210F Autophagy protein 5 - APG5-like; Apoptosis-specific protein Polyclonal 0.05 mg
15-288-22210F Autophagy protein 5 - APG5-like; Apoptosis-specific protein Polyclonal 0.1 mg
10-288-22210F Autophagy protein 5 - APG5-like; Apoptosis-specific protein 0.05 mg
10-288-22210F Autophagy protein 5 - APG5-like; Apoptosis-specific protein 0.1 mg
3886BP-50 Apg5-Atg Blocking Peptide target: Apg5-Atg 50 μg
46116 Protein,APG5 Human 0.01 mg
46116 Protein,APG5 Human 0.002 mg
46116 Protein,APG5 Human 1 mg
EIAAB24948 Autophagy-related protein LC3 A,Autophagy-related ubiquitin-like modifier LC3 A,MAP1 light chain 3-like protein 1,MAP1A_MAP1B LC3 A,MAP1A_MAP1B light chain 3 A,Map1lc3a,Microtubule-associated protein
EIAAB24949 Autophagy-related protein LC3 A,Autophagy-related ubiquitin-like modifier LC3 A,MAP1 light chain 3-like protein 1,MAP1A_MAP1B LC3 A,MAP1A_MAP1B light chain 3 A,Map1lc3a,Microtubule-associated protein
EIAAB24955 Autophagy-related protein LC3 C,Autophagy-related ubiquitin-like modifier LC3 C,Homo sapiens,Human,MAP1 light chain 3-like protein 3,MAP1A_MAP1B LC3 C,MAP1A_MAP1B light chain 3 C,MAP1LC3C,Microtubule-
EIAAB24954 Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,Homo sapiens,Human,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,MAP1ALC3,MAP1LC3B,Mic
EIAAB24950 Autophagy-related protein LC3 A,Autophagy-related ubiquitin-like modifier LC3 A,Homo sapiens,Human,MAP1 light chain 3-like protein 1,MAP1A_MAP1B LC3 A,MAP1A_MAP1B light chain 3 A,MAP1LC3A,Microtubule-
EIAAB24952 Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,Bos taurus,Bovine,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,MAP1ALC3,MAP1LC3,MAP1L
EIAAB24953 Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,Map1alc3,Map1lc3,Map1lc3b,Microtubule-as
EIAAB24951 Autophagy-related protein LC3 B,Autophagy-related ubiquitin-like modifier LC3 B,MAP1 light chain 3-like protein 2,MAP1A_MAP1B LC3 B,MAP1A_MAP1B light chain 3 B,Map1alc3,Map1lc3,Map1lc3b,Microtubule-as
EIAAB24947 Autophagy-related protein LC3 A,Autophagy-related ubiquitin-like modifier LC3 A,Bos taurus,Bovine,MAP1 light chain 3-like protein 1,MAP1A_MAP1B LC3 A,MAP1A_MAP1B light chain 3 A,MAP1LC3A,Microtubule-a
EIAAB11897 Damage-regulated autophagy modulator,DNA damage-regulated autophagy modulator protein 1,DRAM,DRAM1,Homo sapiens,Human
EIAAB11896 Damage-regulated autophagy modulator,DNA damage-regulated autophagy modulator protein 1,Dram,Dram1,Mouse,Mus musculus
18-003-43321 Cysteine protease ATG4B - EC 3.4.22.-; Autophagy-related protein 4 homolog B; hAPG4B; Autophagin-1; Autophagy-related cysteine endopeptidase 1; AUT-like 1 cysteine endopeptidase Polyclonal 0.05 mg Aff Pur
26-750 TMEM74 plays an essential role in autophagy. TMEM74-induced autophagy may involve PI3K signal transduction. 0.05 mg
Autophagy Autophagy ,AT1H2:2 SignArrays
28-091 Autophagy is the process by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is postulated to be essential for cell homeostasis and cell remodeling during diff 0.05 mg
28-092 Autophagy is the process by which endogenous proteins and damaged organelles are destroyed intracellularly. Autophagy is postulated to be essential for cell homeostasis and cell remodeling during diff 0.1 mg


 

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