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Vesicle-fusing ATPase (EC 3.6.4.6) (N-ethylmaleimide-sensitive fusion protein) (NEM-sensitive fusion protein) (Vesicular-fusion protein NSF)

 NSF_HUMAN               Reviewed;         744 AA.
P46459; A8K2D9; B4DFA2; Q8N6D7; Q9UKZ2;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 3.
22-NOV-2017, entry version 179.
RecName: Full=Vesicle-fusing ATPase;
EC=3.6.4.6;
AltName: Full=N-ethylmaleimide-sensitive fusion protein;
Short=NEM-sensitive fusion protein;
AltName: Full=Vesicular-fusion protein NSF;
Name=NSF;
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=Brain;
Hong R., Moriyama Y., Mori H., Futai M., Yamamoto A., Tashiro Y.,
Fukui T., Tagaya M.;
"Structure and localization of a brain N-ethylmaleimide-sensitive
factor involved in vesicular transport.";
Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Bui T.D., Lu L., Hong W.;
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Zhang R., Liu Z., Wu M.;
"The regulation of hNSF gene expression.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum, and Thalamus;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the
fusion of transport vesicles within the Golgi cisternae. Is also
required for transport from the endoplasmic reticulum to the Golgi
stack. Seems to function as a fusion protein required for the
delivery of cargo proteins to all compartments of the Golgi stack
independent of vesicle origin. Interaction with AMPAR subunit
GRIA2 leads to influence GRIA2 membrane cycling (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P18708};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:P18708};
-!- SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2.
Interacts with GRIA2. Interacts with PLK2, leading to disrupt the
interaction with GRIA2. Interacts with MUSK; may regulate MUSK
endocytosis and activity (By similarity). Interacts with CDK16 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q9UBS5:GABBR1; NbExp=3; IntAct=EBI-712251, EBI-724156;
O75899:GABBR2; NbExp=4; IntAct=EBI-712251, EBI-715469;
P42262:GRIA2; NbExp=2; IntAct=EBI-712251, EBI-3909876;
P54920:NAPA; NbExp=2; IntAct=EBI-712251, EBI-749652;
P43378:PTPN9; NbExp=2; IntAct=EBI-712251, EBI-742898;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P46459-1; Sequence=Displayed;
Name=2;
IsoId=P46459-2; Sequence=VSP_056420, VSP_056421;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation at Ser-569 interferes with
homohexamerization. {ECO:0000250}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA17411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U03985; AAA17411.1; ALT_INIT; mRNA.
EMBL; AF135168; AAF70545.1; -; mRNA.
EMBL; AF102846; AAF04745.2; -; mRNA.
EMBL; AK290204; BAF82893.1; -; mRNA.
EMBL; AK294001; BAG57363.1; -; mRNA.
EMBL; AC004098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC138688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC217769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC217778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC217780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030613; AAH30613.1; -; mRNA.
CCDS; CCDS42354.1; -. [P46459-1]
PIR; G01234; G01234.
RefSeq; NP_006169.2; NM_006178.3. [P46459-1]
UniGene; Hs.431279; -.
ProteinModelPortal; P46459; -.
SMR; P46459; -.
BioGrid; 110960; 71.
IntAct; P46459; 47.
MINT; MINT-1369243; -.
STRING; 9606.ENSP00000381293; -.
ChEMBL; CHEMBL2311231; -.
TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
iPTMnet; P46459; -.
PhosphoSitePlus; P46459; -.
SwissPalm; P46459; -.
BioMuta; NSF; -.
DMDM; 257051048; -.
UCD-2DPAGE; P46459; -.
EPD; P46459; -.
MaxQB; P46459; -.
PaxDb; P46459; -.
PeptideAtlas; P46459; -.
PRIDE; P46459; -.
Ensembl; ENST00000398238; ENSP00000381293; ENSG00000073969. [P46459-1]
Ensembl; ENST00000611398; ENSP00000478614; ENSG00000278174. [P46459-1]
Ensembl; ENST00000620290; ENSP00000481714; ENSG00000276262. [P46459-1]
GeneID; 4905; -.
KEGG; hsa:4905; -.
UCSC; uc002iku.4; human. [P46459-1]
CTD; 4905; -.
DisGeNET; 4905; -.
EuPathDB; HostDB:ENSG00000073969.18; -.
GeneCards; NSF; -.
H-InvDB; HIX0013914; -.
H-InvDB; HIX0013915; -.
HGNC; HGNC:8016; NSF.
HPA; CAB009324; -.
HPA; CAB013645; -.
HPA; HPA003154; -.
HPA; HPA071089; -.
MIM; 601633; gene.
neXtProt; NX_P46459; -.
OpenTargets; ENSG00000073969; -.
PharmGKB; PA31793; -.
eggNOG; KOG0741; Eukaryota.
eggNOG; COG0464; LUCA.
GeneTree; ENSGT00530000064085; -.
HOGENOM; HOG000198544; -.
HOVERGEN; HBG000324; -.
InParanoid; P46459; -.
KO; K06027; -.
OMA; IDWVPIG; -.
OrthoDB; EOG091G02LU; -.
PhylomeDB; P46459; -.
TreeFam; TF300371; -.
Reactome; R-HSA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-6811438; Intra-Golgi traffic.
Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
SIGNOR; P46459; -.
ChiTaRS; NSF; human.
GeneWiki; N-ethylmaleimide_sensitive_fusion_protein; -.
GenomeRNAi; 4905; -.
PMAP-CutDB; P46459; -.
PRO; PR:P46459; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000073969; -.
CleanEx; HS_NSF; -.
ExpressionAtlas; P46459; baseline and differential.
Genevisible; P46459; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043198; C:dendritic shaft; ISS:ParkinsonsUK-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0005795; C:Golgi stack; ISS:ParkinsonsUK-UCL.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0042623; F:ATPase activity, coupled; IEA:Ensembl.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
GO; GO:0017137; F:Rab GTPase binding; ISS:ParkinsonsUK-UCL.
GO; GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL.
GO; GO:0017075; F:syntaxin-1 binding; ISS:ParkinsonsUK-UCL.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0006887; P:exocytosis; TAS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IMP:CACAO.
GO; GO:0045026; P:plasma membrane fusion; TAS:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:CACAO.
GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
GO; GO:0017157; P:regulation of exocytosis; ISS:ParkinsonsUK-UCL.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
GO; GO:0035494; P:SNARE complex disassembly; ISS:ParkinsonsUK-UCL.
GO; GO:0016192; P:vesicle-mediated transport; ISS:ParkinsonsUK-UCL.
Gene3D; 3.10.330.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR004201; Cdc48_dom2.
InterPro; IPR029067; CDC48_domain_2-like_sf.
InterPro; IPR003338; CDC4_N-term_subdom.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00004; AAA; 2.
Pfam; PF02933; CDC48_2; 1.
Pfam; PF02359; CDC48_N; 1.
SMART; SM00382; AAA; 2.
SMART; SM01072; CDC48_2; 1.
SMART; SM01073; CDC48_N; 1.
SUPFAM; SSF50692; SSF50692; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54585; SSF54585; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
Repeat; Transport.
CHAIN 1 744 Vesicle-fusing ATPase.
/FTId=PRO_0000084563.
NP_BIND 505 510 ATP. {ECO:0000250|UniProtKB:P18708}.
NP_BIND 545 552 ATP. {ECO:0000250|UniProtKB:P18708}.
METAL 550 550 Magnesium.
{ECO:0000250|UniProtKB:P18708}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000250|UniProtKB:P46460}.
MOD_RES 207 207 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 259 259 Phosphotyrosine.
{ECO:0000250|UniProtKB:P46460}.
MOD_RES 569 569 Phosphoserine; by CDK16.
{ECO:0000250|UniProtKB:P46460}.
VAR_SEQ 1 94 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056420.
VAR_SEQ 739 744 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056421.
VARIANT 476 476 T -> M (in dbSNP:rs155733).
/FTId=VAR_029580.
CONFLICT 22 22 A -> S (in Ref. 1; AAA17411 and 2;
AAF70545). {ECO:0000305}.
CONFLICT 25 25 N -> S (in Ref. 4; BAF82893).
{ECO:0000305}.
CONFLICT 107 107 I -> N (in Ref. 1; AAA17411, 2; AAF70545
and 3; AAF04745). {ECO:0000305}.
CONFLICT 130 130 F -> Y (in Ref. 1; AAA17411, 2; AAF70545
and 3; AAF04745). {ECO:0000305}.
CONFLICT 154 154 A -> S (in Ref. 1; AAA17411, 2; AAF70545
and 3; AAF04745). {ECO:0000305}.
CONFLICT 237 237 S -> F (in Ref. 1; AAA17411, 2; AAF70545
and 3; AAF04745). {ECO:0000305}.
CONFLICT 251 251 K -> I (in Ref. 1; AAA17411, 2; AAF70545
and 3; AAF04745). {ECO:0000305}.
CONFLICT 427 427 K -> R (in Ref. 4; BAF82893).
{ECO:0000305}.
CONFLICT 571 571 D -> E (in Ref. 3; AAF04745).
{ECO:0000305}.
CONFLICT 639 639 K -> M (in Ref. 4; BAF82893).
{ECO:0000305}.
CONFLICT 686 686 F -> L (in Ref. 1; AAA17411, 2; AAF70545
and 3; AAF04745). {ECO:0000305}.
SEQUENCE 744 AA; 82594 MW; BF545A2A0C7EC2F7 CRC64;
MAGRSMQAAR CPTDELSLTN CAVVNEKDFQ SGQHVIVRTS PNHRYTFTLK THPSVVPGSI
AFSLPQRKWA GLSIGQEIEV SLYTFDKAKQ CIGTMTIEID FLQKKSIDSN PYDTDKMAAE
FIQQFNNQAF SVGQQLVFSF NEKLFGLLVK DIEAMDPSIL KGEPATGKRQ KIEVGLVVGN
SQVAFEKAEN SSLNLIGKAK TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF
PPEIVEQMGC KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG
VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL
SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF
LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL
LEGPPHSGKT ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD VLQEMEMLNA
FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG KKVWIGIKKL LMLIEMSLQM
DPEYRVRKFL ALLREEGASP LDFD


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orb80257 Human Angiopoietin-like Protein 4 protein The ANGPTL4 Human Recombinant is manufactured with N-terminal fusion of His Tag. The Angiopoietin-like Protein His -Tagged Fusion Protein is 25 kDa protein co 2
orb80256 Human Angiopoietin-like protein The ANGPTL3 Human Recombinant is produced with N-terminal fusion of His-Tag. The Angiopoietin-like protein His Tagged Fusion Protein is 26kDa containing 207 amino acid 2
orb80244 Human Adiponectin His tag protein The Acrp30 Human is created as recombinant protein with N-terminal fusion of His Tag. The Adiponectin His-Tagged Fusion Protein, produced in E.coli, is 26.4 kDa prote 10
orb80258 Human Angiopoietin-like Protein 4 HEK protein The ANGPTL4 Human Recombinant is manufactured with C-terminal fusion of 11 amino acid FLAG Tag. The ANGPTL4 Flag -Tagged Fusion Protein is 44.2kDa protein 2
H-3588.0500 Human Parainfluenza Virus Type 3 Fusion Protein (454_488) (acetylated) Salt _ Binding _ Synonym HPIV_3 Fusion Protein (454_488) (acetylated) SumFormula C183H294N54O59 0.5 mg
H-3588.1000 Human Parainfluenza Virus Type 3 Fusion Protein (454_488) (acetylated) Salt _ Binding _ Synonym HPIV_3 Fusion Protein (454_488) (acetylated) SumFormula C183H294N54O59 1.0 mg
orb80626 Human TNF Ligand Superfamily Member 12 protein The TWEAK Human Recombinant is manufactured with N-terminal fusion of 13 amino acid FLAG Tag. The TNFSF12 Flag -Tagged Fusion Protein has Mw of 18.7kDa c 5
orb81314 Human Regenerating Islet-Derived 4 protein The Recombinant Human REG-4 is manufactured with N-terminal fusion of His Tag. The Recombinant Human REG-IV His-Tagged Fusion Protein is 17.4 kDa protein con 2
orb80595 Rat Resistin protein Resistin Rat Recombinant is manufactured with N-terminal fusion of His tag. Resistin Rat Recombinant His-Tagged Fusion Protein is an 11.9 kDa protein containing 94 amino acid resi 5
EIAAB38987 Bos taurus,Bovine,SNAP29,SNAP-29,Soluble 29 kDa NSF attachment protein,Synaptosomal-associated protein 29,Vesicle-membrane fusion protein SNAP-29


 

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