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Coatomer subunit gamma (Gamma-coat protein) (Gamma-COP)

 COPG_DROME              Reviewed;         883 AA.
Q8I0G5; E1JJ29; Q8MYW4; Q9U677; Q9V9W9;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 128.
RecName: Full=Coatomer subunit gamma {ECO:0000250|UniProtKB:P53620, ECO:0000312|EMBL:AAN14275.1};
AltName: Full=Gamma-coat protein {ECO:0000250|UniProtKB:P53620};
Short=Gamma-COP {ECO:0000250|UniProtKB:P53620};
Name=gammaCOP {ECO:0000312|FlyBase:FBgn0028968};
Synonyms=copg {ECO:0000312|EMBL:AAF05719.1}, gamma-Cop;
ORFNames=CG1528 {ECO:0000312|FlyBase:FBgn0028968};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305, ECO:0000312|EMBL:AAF05719.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
STRAIN=Berkeley {ECO:0000269|PubMed:11018518};
TISSUE=Larva {ECO:0000269|PubMed:11018518}, and
Pupae {ECO:0000269|PubMed:11018518};
PubMed=11018518; DOI=10.1016/S0014-5793(00)02033-0;
Hahn Y., Lee Y.J., Yun J.H., Yang S.K., Park C.W., Mita K., Huh T.-L.,
Rhee M., Chung J.H.;
"Duplication of genes encoding non-clathrin coat protein gamma-COP in
vertebrate, insect and plant evolution.";
FEBS Lett. 482:31-36(2000).
[2] {ECO:0000312|EMBL:AAN14275.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3] {ECO:0000305, ECO:0000312|EMBL:AAN14275.1}
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4] {ECO:0000305, ECO:0000312|EMBL:AAN71383.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Embryo {ECO:0000269|PubMed:12537569};
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5] {ECO:0000305}
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=16169286; DOI=10.1016/j.modgep.2005.06.001;
Grieder N.C., Kloter U., Gehring W.J.;
"Expression of COPI components during development of Drosophila
melanogaster.";
Gene Expr. Patterns 6:11-21(2005).
[6] {ECO:0000305}
FUNCTION.
PubMed=19067489; DOI=10.1371/journal.pbio.0060292;
Beller M., Sztalryd C., Southall N., Bell M., Jackle H., Auld D.S.,
Oliver B.;
"COPI complex is a regulator of lipid homeostasis.";
PLoS Biol. 6:E292-E292(2008).
[7] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=18398480; DOI=10.1371/journal.pone.0001964;
Jayaram S.A., Senti K.A., Tiklova K., Tsarouhas V., Hemphala J.,
Samakovlis C.;
"COPI vesicle transport is a common requirement for tube expansion in
Drosophila.";
PLoS ONE 3:E1964-E1964(2008).
[8] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=18802472; DOI=10.1371/journal.pone.0003241;
Grieder N.C., Caussinus E., Parker D.S., Cadigan K., Affolter M.,
Luschnig S.;
"gammaCOP is required for apical protein secretion and epithelial
morphogenesis in Drosophila melanogaster.";
PLoS ONE 3:E3241-E3241(2008).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins. Required for limiting lipid
storage in lipid droplets. Involved in the expansion of luminal
extracellular matrices and apical membrane during tubulogenesis.
Required in the tracheal epithelium for luminal protein secretion
and diametric tube growth. In salivary glands, required for
deposition of O-glycans and luminal extracellular matrix assembly.
Required for epidermal morphogenesis and cuticle development.
{ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472,
ECO:0000269|PubMed:19067489}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits.
{ECO:0000250|UniProtKB:P32074, ECO:0000250|UniProtKB:P53620,
ECO:0000250|UniProtKB:P53622}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32074,
ECO:0000250|UniProtKB:P53620, ECO:0000250|UniProtKB:P53622}. Golgi
apparatus membrane {ECO:0000269|PubMed:18398480,
ECO:0000269|PubMed:18802472}; Peripheral membrane protein
{ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472};
Cytoplasmic side {ECO:0000269|PubMed:18398480,
ECO:0000269|PubMed:18802472}. Cytoplasmic vesicle, COPI-coated
vesicle membrane {ECO:0000269|PubMed:18398480,
ECO:0000269|PubMed:18802472}; Peripheral membrane protein
{ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472};
Cytoplasmic side {ECO:0000269|PubMed:18398480,
ECO:0000269|PubMed:18802472}. Endoplasmic reticulum
{ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472}.
Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
side of the Golgi, as well as on the vesicles/buds originating
from it. {ECO:0000250|UniProtKB:P32074,
ECO:0000250|UniProtKB:P53620, ECO:0000250|UniProtKB:P53622,
ECO:0000269|PubMed:18398480, ECO:0000269|PubMed:18802472}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=B {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:12537569};
IsoId=Q8I0G5-1; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=A {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:11018518};
IsoId=Q8I0G5-2; Sequence=VSP_040672;
Note=No experimental confirmation available. {ECO:0000305};
Name=C {ECO:0000269|PubMed:10731132, ECO:0000269|PubMed:12537569};
IsoId=Q8I0G5-3; Sequence=VSP_040672, VSP_040673;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in ovary, testis, testis tip, young
spermatocytes, germ cells and follicle cells. Up-regulated
expression within centrally to posteriorly located germarial cysts
and in migrating follicle cells. Widespread expression in imaginal
disks including eye-antennal disk, wing disk, third leg and
haltere disk. {ECO:0000269|PubMed:16169286}.
-!- DEVELOPMENTAL STAGE: Expressed during spermatogenesis and at later
stages of oogenesis. During embryonic and larval development,
expressed ubiquitously. Starting at stage 10 embryos and lasting
until the end of embryonic development, strongly expressed in the
salivary glands and in cells of the presumptive proventriculus.
Maternal expression abundant in early embryos. Zygotic expression
commences in the epidermis and salivary glands from stage 11,
initiates in the trachea at stage 13, and at early stage 15 is
also detected in the foregut and hindgut tubes.
{ECO:0000269|PubMed:16169286, ECO:0000269|PubMed:18398480}.
-!- DISRUPTION PHENOTYPE: Narrow tracheal tubes and thin salivary
glands with reduced tube diameter and impaired tube elongation.
Fails to complete dorsal closure. Fails to efficiently secrete
luminal components and assemble the luminal chitinous matrix
during tracheal tube expansion. In salivary glands, fails in the
luminal deposition and assembly of a distinct, transient
intraluminal matrix. Disrupted endoplasmic reticulum and Golgi in
embryos. Null mutants die late in embryogenesis with a poorly
differentiated cuticle and denticle. Defects in cell
rearrangements, in branch elongation, in tube dilation and tube
fusion. {ECO:0000269|PubMed:18398480,
ECO:0000269|PubMed:18802472}.
-!- SIMILARITY: Belongs to the COPG family. {ECO:0000255}.
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EMBL; AF191563; AAF05719.1; -; mRNA.
EMBL; AE014297; AAN14275.1; -; Genomic_DNA.
EMBL; AE014297; AAF57160.1; -; Genomic_DNA.
EMBL; AE014297; ACZ95077.1; -; Genomic_DNA.
EMBL; AY113545; AAM29550.1; -; mRNA.
EMBL; BT001628; AAN71383.1; -; mRNA.
RefSeq; NP_001163784.1; NM_001170313.1. [Q8I0G5-3]
RefSeq; NP_524608.1; NM_079869.3. [Q8I0G5-2]
RefSeq; NP_733432.1; NM_170553.2. [Q8I0G5-1]
UniGene; Dm.1895; -.
ProteinModelPortal; Q8I0G5; -.
BioGrid; 68560; 6.
IntAct; Q8I0G5; 27.
MINT; MINT-1018880; -.
STRING; 7227.FBpp0303129; -.
PaxDb; Q8I0G5; -.
PRIDE; Q8I0G5; -.
EnsemblMetazoa; FBtr0085793; FBpp0085154; FBgn0028968. [Q8I0G5-2]
EnsemblMetazoa; FBtr0085794; FBpp0085155; FBgn0028968. [Q8I0G5-1]
EnsemblMetazoa; FBtr0301290; FBpp0290505; FBgn0028968. [Q8I0G5-3]
GeneID; 43717; -.
KEGG; dme:Dmel_CG1528; -.
UCSC; CG1528-RA; d. melanogaster.
UCSC; CG1528-RB; d. melanogaster. [Q8I0G5-1]
CTD; 43717; -.
FlyBase; FBgn0028968; gammaCOP.
eggNOG; KOG1078; Eukaryota.
eggNOG; COG5240; LUCA.
GeneTree; ENSGT00390000016313; -.
HOGENOM; HOG000250272; -.
InParanoid; Q8I0G5; -.
KO; K17267; -.
OrthoDB; EOG091G0HWQ; -.
PhylomeDB; Q8I0G5; -.
Reactome; R-DME-6807878; COPI-mediated anterograde transport.
Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
GenomeRNAi; 43717; -.
PRO; PR:Q8I0G5; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0028968; -.
ExpressionAtlas; Q8I0G5; differential.
Genevisible; Q8I0G5; DM.
GO; GO:0036063; C:acroblast; IDA:FlyBase.
GO; GO:0005801; C:cis-Golgi network; IDA:FlyBase.
GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:FlyBase.
GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0035147; P:branch fusion, open tracheal system; IMP:FlyBase.
GO; GO:0008362; P:chitin-based embryonic cuticle biosynthetic process; IMP:FlyBase.
GO; GO:0030198; P:extracellular matrix organization; IMP:FlyBase.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0007436; P:larval salivary gland morphogenesis; IMP:FlyBase.
GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
GO; GO:0006909; P:phagocytosis; IMP:FlyBase.
GO; GO:0009306; P:protein secretion; IMP:FlyBase.
GO; GO:0010883; P:regulation of lipid storage; IDA:FlyBase.
GO; GO:0035158; P:regulation of tube diameter, open tracheal system; IMP:FlyBase.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 2.60.40.1480; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR013041; Clathrin_app_Ig-like_sf.
InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
InterPro; IPR032154; Coatomer_g_Cpla.
InterPro; IPR017106; Coatomer_gsu.
InterPro; IPR013040; Coatomer_gsu_app_Ig-like_dom.
InterPro; IPR037067; Coatomer_gsu_app_sf.
PANTHER; PTHR10261; PTHR10261; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF16381; Coatomer_g_Cpla; 1.
Pfam; PF08752; COP-gamma_platf; 1.
PIRSF; PIRSF037093; Coatomer_gamma_subunit; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49348; SSF49348; 1.
SUPFAM; SSF55711; SSF55711; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
Golgi apparatus; Membrane; Protein transport; Reference proteome;
Repeat; Transport.
CHAIN 1 883 Coatomer subunit gamma.
/FTId=PRO_0000405327.
REPEAT 69 106 HEAT 1.
REPEAT 292 329 HEAT 2.
REPEAT 331 364 HEAT 3.
REPEAT 365 401 HEAT 4.
REPEAT 404 439 HEAT 5.
REPEAT 476 513 HEAT 6.
VAR_SEQ 2 17 NYFSLTSHKKHRGHPS -> GSFRREKDDEED (in
isoform A and isoform C).
{ECO:0000303|PubMed:10731132,
ECO:0000303|PubMed:11018518,
ECO:0000303|PubMed:12537569}.
/FTId=VSP_040672.
VAR_SEQ 18 18 Missing (in isoform C).
{ECO:0000303|PubMed:10731132,
ECO:0000303|PubMed:12537569}.
/FTId=VSP_040673.
CONFLICT 280 280 A -> V (in Ref. 1; AAF05719).
{ECO:0000305}.
CONFLICT 546 546 S -> W (in Ref. 4; AAM29550).
{ECO:0000305}.
CONFLICT 724 724 A -> T (in Ref. 4; AAM29550).
{ECO:0000305}.
CONFLICT 729 729 T -> A (in Ref. 4; AAM29550).
{ECO:0000305}.
CONFLICT 771 771 I -> V (in Ref. 4; AAM29550).
{ECO:0000305}.
SEQUENCE 883 AA; 97690 MW; 7C610B0F7A39692F CRC64;
MNYFSLTSHK KHRGHPSAGP SNAYQNLEKT SVLQETRTFN ETPVNPRKCI HILTKILYLI
NQGEQLVARE ATDCFFAMTK LFQSKDVVLR RMVYLGIKEL SSIAEDVIIV TSSLTKDMTG
KEDLYRAAAI RALCSITDNT MLQAVERYMK QCIVDKNAAV SCAALVSSLR LANTAGDVVK
RWANEAQEAL NSDNIMVQYH ALGLLYHIRK SDRLAVSKLV NKLTRGSLKS PYAVCMLIRI
ACKLIEEEDI PSEELSDSPL FTFIESCLRH KSEMVIYEAA HAIVNLKNTN PRMLSPAFSI
LQLFCSSPKA TLRFAAVRTL NKVAMTHPAA VTTCNLDLEG LITDSNRSVA TLAITTLLKT
GAESSVERLM KQISTFVAEI SDEFKVVVVQ AICALCTKYP RKHTVLMNFL SGMLREEGGL
EYKTSIVDTI ITIIEENADA KESGLSHLCE FIEDCEHVSL AVRILHLLGK EGPFAATPSK
YIRFIYNRVI LESPIVRAAA VTAMAQFGAS CPALLSNILV LLGRCQMDPD DEVRDRATYY
LSILNSERPE LYKNYIIERE NCSLALLEKS LVEHLNGDVD TRFDISIVPK AAIVKPVIAN
DVMLVTSSAP RPPKITREEE SAARLAQLPG IQVLGPIHRS TAPIQLTESE TEYTVQCIKH
IFGQHVVFQF DCLNTLSDQI LENVRVELTL PEGFTTRAVI PCPKLPYNDL QTTFVIVEFP
PDAANSIATF GATLRFVVKD CDPNTGEPES EEGYDDEYML EDLELTVADQ IQKTRKNNFQ
VSWDAADSEE WLQAEDTFVL SAVTTLQDAV NTIVKILGLG AANLSENVPE GTHLHTLLCS
GTFRGGAEIL VRAKLALSEG VTLNLTVRST DQDVAELITA AIG


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EIAAB37640 Amiloride-sensitive sodium channel subunit gamma,Epithelial Na(+) channel subunit gamma,Gamma-ENaC,Gamma-NaCH,Mouse,Mus musculus,Nonvoltage-gated sodium channel 1 subunit gamma,SCNEG,Scnn1g
E2207m ELISA kit Lamb-2,Lamc1,Lamc-1,Laminin B2 chain,Laminin subunit gamma-1,Laminin-1 subunit gamma,Laminin-10 subunit gamma,Laminin-11 subunit gamma,Laminin-2 subunit gamma,Laminin-3 subunit gamma,Lamini 96T
EIAAB26932 I-kappa-B kinase subunit gamma,IkB kinase subunit gamma,IkB kinase-associated protein 1,Ikbkg,IKKAP1,IKKG,IKK-gamma,Inhibitor of nuclear factor kappa-B kinase subunit gamma,mFIP-3,Mouse,Mus musculus,N
U2207h CLIA kit Homo sapiens,Human,LAMB2,LAMC1,Laminin B2 chain,Laminin subunit gamma-1,Laminin-1 subunit gamma,Laminin-10 subunit gamma,Laminin-11 subunit gamma,Laminin-2 subunit gamma,Laminin-3 subunit ga 96T
E2207h ELISA kit Homo sapiens,Human,LAMB2,LAMC1,Laminin B2 chain,Laminin subunit gamma-1,Laminin-1 subunit gamma,Laminin-10 subunit gamma,Laminin-11 subunit gamma,Laminin-2 subunit gamma,Laminin-3 subunit g 96T
EIAAB41761 CCT3,CCTG,CCT-gamma,Matricin,Pig,Sus scrofa,T-complex protein 1 subunit gamma,TCP-1-gamma
EIAAB41759 Cct3,Cctg,CCT-gamma,Matricin,Mouse,mTRiC-P5,Mus musculus,T-complex protein 1 subunit gamma,TCP-1-gamma
EIAAB06090 CACNG6,CACNG8,Homo sapiens,Human,Neuronal voltage-gated calcium channel gamma-8 subunit,TARP gamma-8,Transmembrane AMPAR regulatory protein gamma-8,Voltage-dependent calcium channel gamma-8 subunit


 

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