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Chaperone protein ClpC1, chloroplastic (ATP-dependent Clp protease ATP-binding subunit ClpC homolog 1) (Casein lytic proteinase C1) (Protein DE-REGULATED CAO ACCUMULATION 1) (Protein IRON-RESCUED MUTANT 1)

 CLPC1_ARATH             Reviewed;         929 AA.
Q9FI56; O48931;
21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-APR-2018, entry version 117.
RecName: Full=Chaperone protein ClpC1, chloroplastic {ECO:0000303|PubMed:11299370};
AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC homolog 1;
AltName: Full=Casein lytic proteinase C1;
AltName: Full=Protein DE-REGULATED CAO ACCUMULATION 1;
AltName: Full=Protein IRON-RESCUED MUTANT 1;
Flags: Precursor;
Name=CLPC1 {ECO:0000303|PubMed:11299370};
Synonyms=DCA1, HSP93-V {ECO:0000303|PubMed:22353577}, IRM1;
OrderedLocusNames=At5g50920 {ECO:0000312|Araport:AT5G50920};
ORFNames=K3K7.7 {ECO:0000312|EMBL:BAB08738.1};
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND INDUCTION.
PubMed=11982939; DOI=10.1034/j.1399-3054.2002.1140113.x;
Zheng B., Halperin T., Hruskova-Heidingsfeldova O., Adam Z.,
Clarke A.K.;
"Characterization of chloroplast Clp proteins in Arabidopsis:
localization, tissue specificity and stress responses.";
Physiol. Plantarum 114:92-101(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10470850; DOI=10.1093/dnares/6.3.183;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IX.
Sequence features of the regions of 1,011,550 bp covered by seventeen
P1 and TAC clones.";
DNA Res. 6:183-195(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11299370; DOI=10.1104/pp.125.4.1912;
Adam Z., Adamska I., Nakabayashi K., Ostersetzer O., Haussuhl K.,
Manuell A., Zheng B., Vallon O., Rodermel S.R., Shinozaki K.,
Clarke A.K.;
"Chloroplast and mitochondrial proteases in Arabidopsis. A proposed
nomenclature.";
Plant Physiol. 125:1912-1918(2001).
[7]
SUBUNIT, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=14593120; DOI=10.1074/jbc.M309212200;
Peltier J.-B., Ripoll D.R., Friso G., Rudella A., Cai Y.,
Ytterberg J., Giacomelli L., Pillardy J., van Wijk K.J.;
"Clp protease complexes from photosynthetic and non-photosynthetic
plastids and mitochondria of plants, their predicted three-dimensional
structures, and functional implications.";
J. Biol. Chem. 279:4768-4781(2004).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15516497; DOI=10.1104/pp.104.052928;
Constan D., Froehlich J.E., Rangarajan S., Keegstra K.;
"A stromal Hsp100 protein is required for normal chloroplast
development and function in Arabidopsis.";
Plant Physiol. 136:3605-3615(2004).
[9]
DISRUPTION PHENOTYPE.
PubMed=15563614; DOI=10.1104/pp.104.053835;
Sjoegren L.L., MacDonald T.M., Sutinen S., Clarke A.K.;
"Inactivation of the clpC1 gene encoding a chloroplast Hsp100
molecular chaperone causes growth retardation, leaf chlorosis, lower
photosynthetic activity, and a specific reduction in photosystem
content.";
Plant Physiol. 136:4114-4126(2004).
[10]
FUNCTION.
PubMed=15304652; DOI=10.1073/pnas.0402764101;
Park S., Rodermel S.R.;
"Mutations in ClpC2/Hsp100 suppress the requirement for FtsH in
thylakoid membrane biogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 101:12765-12770(2004).
[11]
NOMENCLATURE, AND DISRUPTION PHENOTYPE.
DOI=10.1111/j.1399-3054.2005.00452.x;
Clarke A.K., MacDonald T.M., Sjoegren L.L.;
"The ATP-dependent Clp protease in chloroplasts of higher plants.";
Physiol. Plantarum 123:406-412(2005).
[12]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15659100; DOI=10.1111/j.1365-313X.2004.02307.x;
Kovacheva S., Bedard J., Patel R., Dudley P., Twell D., Rios G.,
Koncz C., Jarvis P.;
"In vivo studies on the roles of Tic110, Tic40 and Hsp93 during
chloroplast protein import.";
Plant J. 41:412-428(2005).
[13]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17376159; DOI=10.1111/j.1365-313X.2007.03060.x;
Kovacheva S., Bedard J., Wardle A., Patel R., Jarvis P.;
"Further in vivo studies on the role of the molecular chaperone,
Hsp93, in plastid protein import.";
Plant J. 50:364-379(2007).
[14]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17291312; DOI=10.1111/j.1365-313X.2006.02996.x;
Nakagawara E., Sakuraba Y., Yamasato A., Tanaka R., Tanaka A.;
"Clp protease controls chlorophyll b synthesis by regulating the level
of chlorophyllide a oxygenase.";
Plant J. 49:800-809(2007).
[15]
INDUCTION.
PubMed=17144892; DOI=10.1111/j.1365-313X.2006.02940.x;
Lee U., Rioflorido I., Hong S.W., Larkindale J., Waters E.R.,
Vierling E.;
"The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress
and chloroplast development.";
Plant J. 49:115-127(2007).
[16]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION
PHENOTYPE, AND MUTAGENESIS OF GLY-773.
PubMed=20382967; DOI=10.1093/aob/mcq051;
Wu H., Ji Y., Du J., Kong D., Liang H., Ling H.Q.;
"ClpC1, an ATP-dependent Clp protease in plastids, is involved in iron
homeostasis in Arabidopsis leaves.";
Ann. Bot. 105:823-833(2010).
[17]
FUNCTION, AND DOMAIN.
PubMed=22353577; DOI=10.1104/pp.112.193300;
Chu C.C., Li H.M.;
"The amino-terminal domain of chloroplast Hsp93 is important for its
membrane association and functions in vivo.";
Plant Physiol. 158:1656-1665(2012).
[18]
REVIEW.
PubMed=22085372; DOI=10.1111/j.1399-3054.2011.01541.x;
Clarke A.K.;
"The chloroplast ATP-dependent Clp protease in vascular plants - new
dimensions and future challenges.";
Physiol. Plantarum 145:235-244(2012).
[19]
TISSUE SPECIFICITY, AND INTERACTION WITH CLPS1.
PubMed=23898032; DOI=10.1105/tpc.113.112557;
Nishimura K., Asakura Y., Friso G., Kim J., Oh S.H., Rutschow H.,
Ponnala L., van Wijk K.J.;
"ClpS1 is a conserved substrate selector for the chloroplast Clp
protease system in Arabidopsis.";
Plant Cell 25:2276-2301(2013).
[20]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24599948; DOI=10.1074/jbc.M113.534552;
Sjoegren L.L., Tanabe N., Lymperopoulos P., Khan N.Z., Rodermel S.R.,
Aronsson H., Clarke A.K.;
"Quantitative analysis of the chloroplast molecular chaperone
ClpC/Hsp93 in Arabidopsis reveals new insights into its localization,
interaction with the Clp proteolytic core, and functional
importance.";
J. Biol. Chem. 289:11318-11330(2014).
[21]
INTERACTION WITH CLPF.
PubMed=26419670; DOI=10.1105/tpc.15.00574;
Nishimura K., Apitz J., Friso G., Kim J., Ponnala L., Grimm B.,
van Wijk K.J.;
"Discovery of a unique Clp Component, ClpF, in chloroplasts: A
proposed binary ClpF-ClpS1 adaptor complex functions in substrate
recognition and delivery.";
Plant Cell 27:2677-2691(2015).
-!- FUNCTION: Molecular chaperone that hydrolyzes ATP and is
associated with the chloroplast protein import apparatus. May
function as the motor for chloroplast protein translocation, as
translocation requires ATP hydrolysis in the stroma. May interact
with a ClpP-like protease involved in degradation of denatured
proteins in the chloroplast. Involved in the regulation of
chlorophyll b biosynthesis through the destabilization of
chlorophyllide a oxygenase (CAO) protein in response to the
accumulation of chlorophyll b. Involved in leaf iron homeostasis.
{ECO:0000269|PubMed:15304652, ECO:0000269|PubMed:15516497,
ECO:0000269|PubMed:15659100, ECO:0000269|PubMed:17291312,
ECO:0000269|PubMed:17376159, ECO:0000269|PubMed:20382967,
ECO:0000269|PubMed:22353577, ECO:0000269|PubMed:24599948}.
-!- SUBUNIT: Homodimer (PubMed:14593120). May form hexamer and
interact with Clp core (PubMed:14593120). Interacts (via N-
terminus) with CLPS1 (PubMed:23898032). Interacts with CLPF
(PubMed:26419670). {ECO:0000269|PubMed:14593120,
ECO:0000269|PubMed:23898032, ECO:0000269|PubMed:26419670}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:11982939, ECO:0000269|PubMed:14593120,
ECO:0000269|PubMed:20382967, ECO:0000269|PubMed:24599948}.
Plastid, chloroplast membrane {ECO:0000269|PubMed:24599948}.
Note=The membrane association is important for the in vivo
functions. {ECO:0000269|PubMed:24599948}.
-!- TISSUE SPECIFICITY: Highly expressed in rosette leaves. Expressed
in roots, stems and inflorescences (PubMed:11982939,
PubMed:15659100, PubMed:20382967). Expressed in photosynthetic
green tissues with high levels in young, developing leaf tissues
(PubMed:23898032). {ECO:0000269|PubMed:11982939,
ECO:0000269|PubMed:15659100, ECO:0000269|PubMed:20382967,
ECO:0000269|PubMed:23898032}.
-!- INDUCTION: By cold and salt stresses. Not induced by heat stress.
{ECO:0000269|PubMed:11982939, ECO:0000269|PubMed:17144892}.
-!- DOMAIN: The N-terminal domain (91-234) is important for membrane
association and is essential for the in vivo functions, but not
for the ATPase activity. {ECO:0000269|PubMed:22353577}.
-!- DISRUPTION PHENOTYPE: Small plants with chlorotic leaves, aberrant
chloroplast biogenesis and inefficient chloroplast import of both
photosynthetic and non-photosynthetic preproteins
(PubMed:15516497, PubMed:15563614, Ref.11, PubMed:15659100,
PubMed:17376159, PubMed:17291312, PubMed:20382967). Clpc1 and
clpc2 double mutants are embryo lethal when homozygous
(PubMed:17376159). {ECO:0000269|PubMed:15516497,
ECO:0000269|PubMed:15563614, ECO:0000269|PubMed:15659100,
ECO:0000269|PubMed:17291312, ECO:0000269|PubMed:17376159,
ECO:0000269|PubMed:20382967, ECO:0000269|Ref.11}.
-!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
{ECO:0000305}.
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EMBL; AF022909; AAC04687.1; -; mRNA.
EMBL; AB017063; BAB08738.1; -; Genomic_DNA.
EMBL; CP002688; AED96011.1; -; Genomic_DNA.
EMBL; AY102125; AAM26692.1; -; mRNA.
EMBL; AK227173; BAE99213.1; -; mRNA.
PIR; T52292; T52292.
RefSeq; NP_568746.1; NM_124471.4.
UniGene; At.24774; -.
UniGene; At.74761; -.
UniGene; At.74764; -.
UniGene; At.75059; -.
PDB; 5GUI; X-ray; 1.20 A; A=94-238.
PDBsum; 5GUI; -.
ProteinModelPortal; Q9FI56; -.
SMR; Q9FI56; -.
BioGrid; 20411; 2.
IntAct; Q9FI56; 1.
STRING; 3702.AT5G50920.1; -.
TCDB; 3.A.9.1.2; the chloroplast envelope protein translocase (cept or tic-toc) family.
PaxDb; Q9FI56; -.
PRIDE; Q9FI56; -.
EnsemblPlants; AT5G50920.1; AT5G50920.1; AT5G50920.
GeneID; 835165; -.
Gramene; AT5G50920.1; AT5G50920.1; AT5G50920.
KEGG; ath:AT5G50920; -.
Araport; AT5G50920; -.
TAIR; locus:2157383; AT5G50920.
eggNOG; KOG1051; Eukaryota.
eggNOG; COG0542; LUCA.
HOGENOM; HOG000218210; -.
InParanoid; Q9FI56; -.
KO; K03696; -.
OMA; FHSKVRQ; -.
OrthoDB; EOG09360210; -.
PhylomeDB; Q9FI56; -.
PRO; PR:Q9FI56; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FI56; baseline and differential.
Genevisible; Q9FI56; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0009532; C:plastid stroma; IDA:TAIR.
GO; GO:0031897; C:Tic complex; TAS:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:TAIR.
GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
GO; GO:0045037; P:protein import into chloroplast stroma; IMP:TAIR.
GO; GO:0045036; P:protein targeting to chloroplast; IMP:TAIR.
GO; GO:0010380; P:regulation of chlorophyll biosynthetic process; IMP:TAIR.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
Gene3D; 1.10.1780.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR019489; Clp_ATPase_C.
InterPro; IPR004176; Clp_N.
InterPro; IPR036628; Clp_N_dom_sf.
InterPro; IPR001270; ClpA/B.
InterPro; IPR018368; ClpA/B_CS1.
InterPro; IPR028299; ClpA/B_CS2.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001943; UVR_dom.
Pfam; PF00004; AAA; 1.
Pfam; PF07724; AAA_2; 1.
Pfam; PF02861; Clp_N; 2.
Pfam; PF10431; ClpB_D2-small; 1.
Pfam; PF02151; UVR; 1.
PRINTS; PR00300; CLPPROTEASEA.
SMART; SM00382; AAA; 2.
SMART; SM01086; ClpB_D2-small; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF81923; SSF81923; 1.
PROSITE; PS00870; CLPAB_1; 1.
PROSITE; PS00871; CLPAB_2; 1.
PROSITE; PS50151; UVR; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Chaperone; Chloroplast; Complete proteome;
Membrane; Nucleotide-binding; Plastid; Protein transport;
Reference proteome; Repeat; Transit peptide; Transport.
TRANSIT 1 38 Chloroplast. {ECO:0000255}.
CHAIN 39 929 Chaperone protein ClpC1, chloroplastic.
/FTId=PRO_0000412575.
DOMAIN 511 546 UVR. {ECO:0000255|PROSITE-
ProRule:PRU00217}.
NP_BIND 302 309 ATP. {ECO:0000255}.
NP_BIND 645 652 ATP. {ECO:0000255}.
REGION 257 504 I. {ECO:0000250}.
REGION 571 762 II. {ECO:0000250}.
MUTAGEN 773 773 G->R: In irm1; iron deficiency chlorosis.
{ECO:0000269|PubMed:20382967}.
CONFLICT 40 48 SQLQVSGLR -> IIFNVWLP (in Ref. 1;
AAC04687). {ECO:0000305}.
CONFLICT 187 188 EA -> AT (in Ref. 1; AAC04687).
{ECO:0000305}.
CONFLICT 507 507 A -> V (in Ref. 1; AAC04687).
{ECO:0000305}.
CONFLICT 685 685 K -> T (in Ref. 1; AAC04687).
{ECO:0000305}.
CONFLICT 690 690 P -> L (in Ref. 1; AAC04687).
{ECO:0000305}.
HELIX 100 115 {ECO:0000244|PDB:5GUI}.
HELIX 123 132 {ECO:0000244|PDB:5GUI}.
HELIX 137 144 {ECO:0000244|PDB:5GUI}.
HELIX 149 160 {ECO:0000244|PDB:5GUI}.
HELIX 175 190 {ECO:0000244|PDB:5GUI}.
STRAND 194 196 {ECO:0000244|PDB:5GUI}.
HELIX 198 208 {ECO:0000244|PDB:5GUI}.
HELIX 212 219 {ECO:0000244|PDB:5GUI}.
HELIX 224 237 {ECO:0000244|PDB:5GUI}.
SEQUENCE 929 AA; 103453 MW; 438DEA514125F0BF CRC64;
MAMATRVLAQ STPPSLACYQ RNVPSRGSGR SRRSVKMMCS QLQVSGLRMQ GFMGLRGNNA
LDTLGKSRQD FHSKVRQAMN VPKGKASRFT VKAMFERFTE KAIKVIMLAQ EEARRLGHNF
VGTEQILLGL IGEGTGIAAK VLKSMGINLK DARVEVEKII GRGSGFVAVE IPFTPRAKRV
LELSLEEARQ LGHNYIGSEH LLLGLLREGE GVAARVLENL GADPSNIRTQ VIRMVGENNE
VTANVGGGSS SNKMPTLEEY GTNLTKLAEE GKLDPVVGRQ PQIERVVQIL GRRTKNNPCL
IGEPGVGKTA IAEGLAQRIA SGDVPETIEG KKVITLDMGL LVAGTKYRGE FEERLKKLME
EIRQSDEIIL FIDEVHTLIG AGAAEGAIDA ANILKPALAR GELQCIGATT LDEYRKHIEK
DPALERRFQP VKVPEPTVDE TIQILKGLRE RYEIHHKLRY TDESLVAAAQ LSYQYISDRF
LPDKAIDLID EAGSRVRLRH AQVPEEAREL EKELRQITKE KNEAVRGQDF EKAGTLRDRE
IELRAEVSAI QAKGKEMSKA ESETGEEGPM VTESDIQHIV SSWTGIPVEK VSTDESDRLL
KMEETLHKRI IGQDEAVKAI SRAIRRARVG LKNPNRPIAS FIFSGPTGVG KSELAKALAA
YYFGSEEAMI RLDMSEFMER HTVSKLIGSP PGYVGYTEGG QLTEAVRRRP YTVVLFDEIE
KAHPDVFNMM LQILEDGRLT DSKGRTVDFK NTLLIMTSNV GSSVIEKGGR RIGFDLDYDE
KDSSYNRIKS LVTEELKQYF RPEFLNRLDE MIVFRQLTKL EVKEIADILL KEVFERLKKK
EIELQVTERF KERVVDEGYN PSYGARPLRR AIMRLLEDSM AEKMLAREIK EGDSVIVDVD
AEGNVTVLNG GSGTPTTSLE EQEDSLPVA


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29-285 ACO1, also known as iron regulatory element binding protein 1 (IREB1), is a cytosolic protein which binds to iron-responsive elements (IREs). It plays a central role in cellular iron homeostasis. It w 0.05 mg
18-003-43581 Iron-responsive element-binding protein 1 - IRE-BP 1; Iron regulatory protein 1; IRP1; Ferritin repressor protein; Aconitate hydratase; EC 4.2.1.3; Citrate hydro-lyase; Aconitase Polyclonal 0.05 mg Aff Pur
EIAAB34392 Fox-1 homolog B,Fox-1 homolog Fxh,Fox2,Fxh,Hexaribonucleotide-binding protein 2,Hrnbp2,Mouse,Mus musculus,Rbfox2,Rbm9,RNA binding protein fox-1 homolog 2,RNA-binding motif protein 9,RNA-binding protei
20-272-191084 PAPP A - Mouse monoclonal [11E4] to PAPP A; EC 3.4.24.79; Pregnancy-associated plasma protein-A; PAPP-A; Insulin-like growth factor-dependent IGF-binding protein 4 protease; IGF-dependent IGFBP-4 prot 0.1 mg
E0800m ELISA kit IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,Mouse,Mus musculus,Pappa,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protei 96T
EIAAB32656 26S protease regulatory subunit 6A,26S proteasome AAA-ATPase subunit RPT5,Proteasome 26S subunit ATPase 3,Psmc3,Rat,Rattus norvegicus,Spermatogenic cell_sperm-associated Tat-binding protein homolog SA
EIAAB32669 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,p45_SUG,Pig,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,PSMC5,Sus scrofa,Tat-binding protein homolog 10,TBP10
E0800h ELISA kit Homo sapiens,Human,IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,PAPPA,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protei 96T
EIAAB09096 Calcium-activated neutral proteinase small subunit,Calcium-dependent protease small subunit,Calcium-dependent protease small subunit 1,Calpain regulatory subunit,Calpain small subunit 1,CANP small sub
EIAAB09094 Calcium-activated neutral proteinase small subunit,Calcium-dependent protease small subunit,Calcium-dependent protease small subunit 1,Calpain regulatory subunit,Calpain small subunit 1,CANP small sub
EIAAB09093 Calcium-activated neutral proteinase small subunit,Calcium-dependent protease small subunit,Calcium-dependent protease small subunit 1,Calpain regulatory subunit,Calpain small subunit 1,CANP small sub
EIAAB09095 Calcium-activated neutral proteinase small subunit,Calcium-dependent protease small subunit,Calcium-dependent protease small subunit 1,Calpain regulatory subunit,Calpain small subunit 1,CANP small sub
EIAAB09092 Calcium-activated neutral proteinase small subunit,Calcium-dependent protease small subunit,Calcium-dependent protease small subunit 1,Calpain regulatory subunit,Calpain small subunit 1,CANP small sub


 

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