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L-tryptophan--pyruvate aminotransferase 1 (EC 2.6.1.27) (EC 2.6.1.99) (Protein CYTOKININ INDUCED ROOT CURLING 1) (Protein SHADE AVOIDANCE 3) (Protein TRANSPORT INHIBITOR RESPONSE 2) (Protein TRYPTOPHAN AMINOTRANSFERASE OF ARABIDOPSIS 1) (Protein WEAK ETHYLENE INSENSITIVE 8) (Tryptophan transaminase)

 TAA1_ARATH              Reviewed;         391 AA.
Q9S7N2;
30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
07-JUN-2017, entry version 98.
RecName: Full=L-tryptophan--pyruvate aminotransferase 1;
EC=2.6.1.27;
EC=2.6.1.99;
AltName: Full=Protein CYTOKININ INDUCED ROOT CURLING 1;
AltName: Full=Protein SHADE AVOIDANCE 3;
AltName: Full=Protein TRANSPORT INHIBITOR RESPONSE 2;
AltName: Full=Protein TRYPTOPHAN AMINOTRANSFERASE OF ARABIDOPSIS 1;
AltName: Full=Protein WEAK ETHYLENE INSENSITIVE 8;
AltName: Full=Tryptophan transaminase;
Name=TAA1; Synonyms=CKRC1, SAV3, TIR2, WEI8;
OrderedLocusNames=At1g70560; ORFNames=F24J13.13, F5A18.26;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[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]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-166 AND
LYS-217.
PubMed=18394997; DOI=10.1016/j.cell.2008.01.047;
Stepanova A.N., Robertson-Hoyt J., Yun J., Benavente L.M., Xie D.Y.,
Dolezal K., Schlereth A., Juergens G., Alonso J.M.;
"TAA1-mediated auxin biosynthesis is essential for hormone crosstalk
and plant development.";
Cell 133:177-191(2008).
[6]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH PYRIDOXAMINE
PHOSPHATE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY SHADE,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-217 AND GLY-250.
PubMed=18394996; DOI=10.1016/j.cell.2008.01.049;
Tao Y., Ferrer J.L., Ljung K., Pojer F., Hong F., Long J.A., Li L.,
Moreno J.E., Bowman M.E., Ivans L.J., Cheng Y., Lim J., Zhao Y.,
Ballare C.L., Sandberg G., Noel J.P., Chory J.;
"Rapid synthesis of auxin via a new tryptophan-dependent pathway is
required for shade avoidance in plants.";
Cell 133:164-176(2008).
[7]
FUNCTION, MUTAGENESIS OF GLY-171, TISSUE SPECIFICITY, INDUCTION BY
AUXIN AND HEAT, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=19625638; DOI=10.1104/pp.109.138859;
Yamada M., Greenham K., Prigge M.J., Jensen P.J., Estelle M.;
"The TRANSPORT INHIBITOR RESPONSE2 gene is required for auxin
synthesis and diverse aspects of plant development.";
Plant Physiol. 151:168-179(2009).
[8]
ENZYME REGULATION.
PubMed=22108404; DOI=10.1105/tpc.111.089029;
He W., Brumos J., Li H., Ji Y., Ke M., Gong X., Zeng Q., Li W.,
Zhang X., An F., Wen X., Li P., Chu J., Sun X., Yan C., Yan N.,
Xie D.Y., Raikhel N., Yang Z., Stepanova A.N., Alonso J.M., Guo H.;
"A small-molecule screen identifies L-kynurenine as a competitive
inhibitor of TAA1/TAR activity in ethylene-directed auxin biosynthesis
and root growth in Arabidopsis.";
Plant Cell 23:3944-3960(2011).
[9]
TISSUE SPECIFICITY, INDUCTION BY ETHYLENE AND CYTOKININ, AND
DISRUPTION PHENOTYPE.
PubMed=21255165; DOI=10.1111/j.1365-313X.2011.04509.x;
Zhou Z.Y., Zhang C.G., Wu L., Zhang C.G., Chai J., Wang M., Jha A.,
Jia P.F., Cui S.J., Yang M., Chen R., Guo G.Q.;
"Functional characterization of the CKRC1/TAA1 gene and dissection of
hormonal actions in the Arabidopsis root.";
Plant J. 66:516-527(2011).
[10]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=22025724; DOI=10.1073/pnas.1108434108;
Mashiguchi K., Tanaka K., Sakai T., Sugawara S., Kawaide H.,
Natsume M., Hanada A., Yaeno T., Shirasu K., Yao H., McSteen P.,
Zhao Y., Hayashi K., Kamiya Y., Kasahara H.;
"The main auxin biosynthesis pathway in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 108:18512-18517(2011).
-!- FUNCTION: L-tryptophan aminotransferase involved in auxin (IAA)
biosynthesis. Can convert L-tryptophan and pyruvate to indole-3-
pyruvic acid (IPA) and alanine. Catalyzes the first step in IPA
branch of the auxin biosynthetic pathway. Required for auxin
production to initiate multiple change in growth in response to
environmental and developmental cues. It is also active with
phenylalanine, tyrosine, leucine, alanine, methionine and
glutamine. Both TAA1 and TAR2 are required for maintaining proper
auxin levels in roots, while TAA1, TAR1 and TAR2 are required for
proper embryo patterning. Involved in the maintenance of the root
stem cell niches and required for shade avoidance.
{ECO:0000269|PubMed:18394996, ECO:0000269|PubMed:18394997,
ECO:0000269|PubMed:19625638, ECO:0000269|PubMed:22025724}.
-!- CATALYTIC ACTIVITY: L-tryptophan + 2-oxoglutarate = (indol-3-
yl)pyruvate + L-glutamate. {ECO:0000269|PubMed:22025724}.
-!- CATALYTIC ACTIVITY: L-tryptophan + pyruvate = indole-3-pyruvate +
L-alanine. {ECO:0000269|PubMed:22025724}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- ENZYME REGULATION: Inhibited by L-kynurenine.
{ECO:0000269|PubMed:22108404}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.29 mM for L-tryptophan {ECO:0000269|PubMed:18394996};
KM=4.74 mM for tyrosine {ECO:0000269|PubMed:18394996};
KM=9.35 mM for phenylalanine {ECO:0000269|PubMed:18394996};
Vmax=25.8 umol/min/ug enzyme with L-tryptophan as substrate
{ECO:0000269|PubMed:18394996};
Vmax=28 umol/min/ug enzyme with tyrosine as substrate
{ECO:0000269|PubMed:18394996};
Vmax=10.6 umol/min/ug enzyme with phenylalanine as substrate
{ECO:0000269|PubMed:18394996};
pH dependence:
Optimum pH is 8.8. {ECO:0000269|PubMed:18394996};
Temperature dependence:
Optimum temperature is 55 degrees Celsius.
{ECO:0000269|PubMed:18394996};
-!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18394996}.
-!- TISSUE SPECIFICITY: Expressed at the leaf margin and in the
vasculature of emerging young leaves. Expressed in the quiescent
center and in the vasculature of root tips. Detected in the shoot
apical meristem, stems, sepals, stamen filaments, the shoot and
root junction, the stigma and the base of the silique.
{ECO:0000269|PubMed:18394996, ECO:0000269|PubMed:19625638,
ECO:0000269|PubMed:21255165}.
-!- DEVELOPMENTAL STAGE: In the heart stage embryo, expressed in the
developing vasculature and the apical epidermal layer. At the
torpedo stage expressed in the developing vasculature of the root,
hypocotyl and cotyledons, as well as in the L1 layer of the
presumptive shoot apical meristem and the adaxial epidermis of the
developing cotyledons. In flowers, the expression is first
restricted to the central outer layers of flower primordia, but
later expands toward the base of gynoecia, becoming limited to two
cell files along the meristematic medial ridge.
{ECO:0000269|PubMed:18394996, ECO:0000269|PubMed:19625638}.
-!- INDUCTION: Up-regulated by trans-zeatin, ethylene and high
temperature. Down-regulated by auxin and shade treatment.
{ECO:0000269|PubMed:18394996, ECO:0000269|PubMed:19625638,
ECO:0000269|PubMed:21255165}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
condition, but exhibits reduced levels of auxin (IAA), reduced
auxin response, reduced sensitivity to ethylene and shorter
hypocotyls and petioles but larger leaf area when grown in
simulated shade. Defective in root gravitropic response and shows
an increased resistance to cytokinin in primary root growth.
{ECO:0000269|PubMed:18394996, ECO:0000269|PubMed:18394997,
ECO:0000269|PubMed:19625638, ECO:0000269|PubMed:21255165}.
-!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC010796; AAG52476.1; -; Genomic_DNA.
EMBL; AC011663; AAG52348.1; -; Genomic_DNA.
EMBL; CP002684; AEE35079.1; -; Genomic_DNA.
EMBL; AK117208; BAC41884.1; -; mRNA.
EMBL; BT005339; AAO63403.1; -; mRNA.
PIR; F96729; F96729.
RefSeq; NP_177213.1; NM_105724.3.
UniGene; At.27817; -.
PDB; 3BWN; X-ray; 2.25 A; A/B/C/D/E/F=1-391.
PDB; 3BWO; X-ray; 2.40 A; A/B/C/D/E/F=1-391.
PDBsum; 3BWN; -.
PDBsum; 3BWO; -.
ProteinModelPortal; Q9S7N2; -.
SMR; Q9S7N2; -.
STRING; 3702.AT1G70560.1; -.
PaxDb; Q9S7N2; -.
EnsemblPlants; AT1G70560.1; AT1G70560.1; AT1G70560.
GeneID; 843393; -.
Gramene; AT1G70560.1; AT1G70560.1; AT1G70560.
KEGG; ath:AT1G70560; -.
Araport; AT1G70560; -.
TAIR; locus:2026826; AT1G70560.
eggNOG; ENOG410II7N; Eukaryota.
eggNOG; ENOG41114NM; LUCA.
HOGENOM; HOG000237549; -.
InParanoid; Q9S7N2; -.
KO; K16903; -.
OMA; CWFLEPS; -.
OrthoDB; EOG09360BJJ; -.
PhylomeDB; Q9S7N2; -.
BioCyc; ARA:AT1G70560-MONOMER; -.
BioCyc; MetaCyc:AT1G70560-MONOMER; -.
BRENDA; 2.6.1.27; 399.
BRENDA; 2.6.1.99; 399.
UniPathway; UPA00151; -.
EvolutionaryTrace; Q9S7N2; -.
PRO; PR:Q9S7N2; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; Q9S7N2; AT.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0080100; F:L-glutamine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0080099; F:L-methionine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0047312; F:L-phenylalanine:pyruvate aminotransferase activity; IDA:TAIR.
GO; GO:0050362; F:L-tryptophan:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0080097; F:L-tryptophan:pyruvate aminotransferase activity; IDA:TAIR.
GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
GO; GO:0080098; F:L-tyrosine:pyruvate aminotransferase activity; IDA:TAIR.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:TAIR.
GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
GO; GO:0042742; P:defense response to bacterium; IGI:TAIR.
GO; GO:0009908; P:flower development; IGI:TAIR.
GO; GO:0048467; P:gynoecium development; IGI:TAIR.
GO; GO:0009684; P:indoleacetic acid biosynthetic process; IMP:TAIR.
GO; GO:0048366; P:leaf development; IMP:TAIR.
GO; GO:0010078; P:maintenance of root meristem identity; IGI:TAIR.
GO; GO:0010087; P:phloem or xylem histogenesis; IGI:TAIR.
GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
GO; GO:0009723; P:response to ethylene; IMP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0009641; P:shade avoidance; IMP:TAIR.
GO; GO:0048367; P:shoot system development; IGI:TAIR.
Gene3D; 2.10.25.30; -; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR006948; Alliinase_C.
InterPro; IPR006947; EGF_alliinase.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
Pfam; PF04864; Alliinase_C; 1.
SUPFAM; SSF53383; SSF53383; 1.
1: Evidence at protein level;
3D-structure; Aminotransferase; Auxin biosynthesis; Complete proteome;
Cytoplasm; Pyridoxal phosphate; Reference proteome; Transferase.
CHAIN 1 391 L-tryptophan--pyruvate aminotransferase
1.
/FTId=PRO_0000401375.
REGION 100 101 Pyridoxal phosphate binding.
REGION 191 194 Pyridoxal phosphate binding.
REGION 214 217 Pyridoxal phosphate binding.
BINDING 58 58 Pyridoxal phosphate.
BINDING 168 168 Pyridoxal phosphate.
BINDING 191 191 Pyridoxal phosphate.
BINDING 225 225 Pyridoxal phosphate.
MOD_RES 217 217 N6-(pyridoxal phosphate)lysine.
{ECO:0000255}.
MUTAGEN 166 166 P->S: In wei8-2; loss of activity.
{ECO:0000269|PubMed:18394997}.
MUTAGEN 171 171 G->E: In tir2-1; loss of activity.
{ECO:0000269|PubMed:19625638}.
MUTAGEN 217 217 K->A: Loss of activity.
{ECO:0000269|PubMed:18394996,
ECO:0000269|PubMed:18394997}.
MUTAGEN 217 217 K->G,R: Reduces growth rate under shade
condition. {ECO:0000269|PubMed:18394996,
ECO:0000269|PubMed:18394997}.
MUTAGEN 250 250 G->S: In sav3-3; reduces growth rate
under shade condition.
{ECO:0000269|PubMed:18394996}.
TURN 20 22 {ECO:0000244|PDB:3BWN}.
HELIX 33 35 {ECO:0000244|PDB:3BWN}.
HELIX 36 41 {ECO:0000244|PDB:3BWN}.
HELIX 43 45 {ECO:0000244|PDB:3BWN}.
STRAND 48 50 {ECO:0000244|PDB:3BWN}.
TURN 52 55 {ECO:0000244|PDB:3BWN}.
STRAND 64 66 {ECO:0000244|PDB:3BWN}.
HELIX 71 84 {ECO:0000244|PDB:3BWN}.
STRAND 90 98 {ECO:0000244|PDB:3BWN}.
HELIX 99 113 {ECO:0000244|PDB:3BWN}.
STRAND 115 124 {ECO:0000244|PDB:3BWN}.
HELIX 131 137 {ECO:0000244|PDB:3BWN}.
STRAND 144 150 {ECO:0000244|PDB:3BWN}.
STRAND 159 166 {ECO:0000244|PDB:3BWN}.
TURN 168 170 {ECO:0000244|PDB:3BWN}.
STRAND 187 191 {ECO:0000244|PDB:3BWN}.
TURN 197 199 {ECO:0000244|PDB:3BWN}.
STRAND 209 214 {ECO:0000244|PDB:3BWN}.
HELIX 215 219 {ECO:0000244|PDB:3BWN}.
HELIX 222 224 {ECO:0000244|PDB:3BWN}.
STRAND 226 231 {ECO:0000244|PDB:3BWN}.
HELIX 234 248 {ECO:0000244|PDB:3BWN}.
HELIX 253 269 {ECO:0000244|PDB:3BWN}.
TURN 275 277 {ECO:0000244|PDB:3BWN}.
HELIX 279 299 {ECO:0000244|PDB:3BWN}.
STRAND 302 305 {ECO:0000244|PDB:3BWN}.
STRAND 312 314 {ECO:0000244|PDB:3BWN}.
TURN 315 318 {ECO:0000244|PDB:3BWN}.
STRAND 319 321 {ECO:0000244|PDB:3BWN}.
STRAND 326 335 {ECO:0000244|PDB:3BWN}.
HELIX 338 344 {ECO:0000244|PDB:3BWN}.
HELIX 352 355 {ECO:0000244|PDB:3BWN}.
STRAND 361 366 {ECO:0000244|PDB:3BWN}.
HELIX 370 381 {ECO:0000244|PDB:3BWN}.
SEQUENCE 391 AA; 44801 MW; 7038D6C93E122614 CRC64;
MVKLENSRKP EKISNKNIPM SDFVVNLDHG DPTAYEEYWR KMGDRCTVTI RGCDLMSYFS
DMTNLCWFLE PELEDAIKDL HGVVGNAATE DRYIVVGTGS TQLCQAAVHA LSSLARSQPV
SVVAAAPFYS TYVEETTYVR SGMYKWEGDA WGFDKKGPYI ELVTSPNNPD GTIRETVVNR
PDDDEAKVIH DFAYYWPHYT PITRRQDHDI MLFTFSKITG HAGSRIGWAL VKDKEVAKKM
VEYIIVNSIG VSKESQVRTA KILNVLKETC KSESESENFF KYGREMMKNR WEKLREVVKE
SDAFTLPKYP EAFCNYFGKS LESYPAFAWL GTKEETDLVS ELRRHKVMSR AGERCGSDKK
HVRVSMLSRE DVFNVFLERL ANMKLIKSID L


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EIAAB37898 Endometrial progesterone-induced protein,EPIP,Oryctolagus cuniculus,Phosphohydroxythreonine aminotransferase,Phosphoserine aminotransferase,PSA,PSAT,PSAT1,Rabbit
E0023h ELISA Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Homo sapiens,Human,TACO,Tryptophan aspartate-containing coat protein 96T
E0023h ELISA kit Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Homo sapiens,Human,TACO,Tryptophan aspartate-containing coat protein 96T
U0023h CLIA Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Homo sapiens,Human,TACO,Tryptophan aspartate-containing coat protein 96T
E0023m ELISA Clipin-A,Coro1,Coro1a,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Mouse,Mus musculus,TACO,Tryptophan aspartate-containing coat protein 96T
E0023m ELISA kit Clipin-A,Coro1,Coro1a,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,Mouse,Mus musculus,TACO,Tryptophan aspartate-containing coat protein 96T
E0023b ELISA Bos taurus,Bovine,Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,TACO,Tryptophan aspartate-containing coat protein 96T
U0023b CLIA Bos taurus,Bovine,Clipin-A,CORO1,CORO1A,Coronin-1A,Coronin-like protein A,Coronin-like protein p57,TACO,Tryptophan aspartate-containing coat protein 96T


 

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