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SNF1-related protein kinase catalytic subunit alpha KIN10 (AKIN10) (EC 2.7.11.1) (AKIN alpha-2) (AKINalpha2)

 KIN10_ARATH             Reviewed;         535 AA.
Q38997; A6XGR0; O04728; Q38987; Q39076; Q8RWD2;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
21-NOV-2003, sequence version 2.
25-APR-2018, entry version 172.
RecName: Full=SNF1-related protein kinase catalytic subunit alpha KIN10;
Short=AKIN10;
EC=2.7.11.1;
AltName: Full=AKIN alpha-2;
Short=AKINalpha2;
Name=KIN10; Synonyms=AK21, SKIN10, SNR2, SNRK1.1;
OrderedLocusNames=At3g01090; ORFNames=T4P13.22;
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 [GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=1339373; DOI=10.1016/0378-1119(92)90100-4;
le Guen L., Thomas M., Bianchi M., Halford N.G., Kreis M.;
"Structure and expression of a gene from Arabidopsis thaliana encoding
a protein related to SNF1 protein kinase.";
Gene 120:249-254(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. Columbia; TISSUE=Seedling;
Lessard P., Kreis M., Thomas M.;
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
Fu H.;
"Functional differentiation of ubiquitin-interacting factors from
Arabidopsis.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-42 (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=7816049; DOI=10.1007/BF00290120;
le Guen L., Thomas M., Kreis M.;
"Gene density and organization in a small region of the Arabidopsis
thaliana genome.";
Mol. Gen. Genet. 245:390-396(1994).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-221.
STRAIN=cv. Eil-0; TISSUE=Leaf;
PubMed=8534852; DOI=10.1007/BF00020984;
Thuemmler F., Kirchner M., Teuber R., Dittrich P.;
"Differential accumulation of the transcripts of 22 novel protein
kinase genes in Arabidopsis thaliana.";
Plant Mol. Biol. 29:551-565(1995).
[9]
FUNCTION, PHOSPHORYLATION, INDUCTION, AND INTERACTION WITH PRL1.
PubMed=10220464; DOI=10.1073/pnas.96.9.5322;
Bhalerao R.P., Salchert K., Bako L., Oekresz L., Szabados L.,
Muranaka T., Machida Y., Schell J., Koncz C.;
"Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like
protein kinases.";
Proc. Natl. Acad. Sci. U.S.A. 96:5322-5327(1999).
[10]
INTERACTION WITH SNF4.
PubMed=10929106; DOI=10.1046/j.1365-313x.2000.00809.x;
Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.;
"Functional identification of an Arabidopsis Snf4 ortholog by
screening for heterologous multicopy suppressors of snf4 deficiency in
yeast.";
Plant J. 23:115-122(2000).
[11]
FUNCTION, AND INTERACTION WITH SKP1 AND PAD1.
PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
Salchert K., del Pozo C., Schell J., Koncz C.;
"SKP1-SnRK protein kinase interactions mediate proteasomal binding of
a plant SCF ubiquitin ligase.";
EMBO J. 20:2742-2756(2001).
[12]
INTERACTION WITH KINB2.
PubMed=11522840; DOI=10.1093/nar/29.17.3685;
Ferrando A., Koncz-Kalman Z., Farras R., Tiburcio A., Schell J.,
Koncz C.;
"Detection of in vivo protein interactions between Snf1-related kinase
subunits with intron-tagged epitope-labelling in plants cells.";
Nucleic Acids Res. 29:3685-3693(2001).
[13]
INTERACTION WITH KINB3.
PubMed=15803412; DOI=10.1007/s11103-004-5111-1;
Gissot L., Polge C., Bouly J.P., Lemaitre T., Kreis M., Thomas M.;
"AKINbeta3, a plant specific SnRK1 protein, is lacking domains present
in yeast and mammals non-catalytic beta-subunits.";
Plant Mol. Biol. 56:747-759(2004).
[14]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-43, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[15]
INTERACTION WITH 5PTASE13, AND SUBCELLULAR LOCATION.
PubMed=18931139; DOI=10.1104/pp.108.130575;
Ananieva E.A., Gillaspy G.E., Ely A., Burnette R.N., Erickson F.L.;
"Interaction of the WD40 domain of a myoinositol polyphosphate 5-
phosphatase with SnRK1 links inositol, sugar, and stress signaling.";
Plant Physiol. 148:1868-1882(2008).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[17]
PHOSPHORYLATION AT THR-198, MUTAGENESIS OF THR-198, AND ENZYME
REGULATION.
PubMed=19339507; DOI=10.1104/pp.108.132787;
Shen W., Reyes M.I., Hanley-Bowdoin L.;
"Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate
SnRK1 by phosphorylating its activation loop.";
Plant Physiol. 150:996-1005(2009).
[18]
FUNCTION, AND MUTAGENESIS OF THR-198.
PubMed=20164192; DOI=10.1074/jbc.M109.079194;
Crozet P., Jammes F., Valot B., Ambard-Bretteville F., Nessler S.,
Hodges M., Vidal J., Thomas M.;
"Cross-phosphorylation between Arabidopsis thaliana sucrose
nonfermenting 1-related protein kinase 1 (AtSnRK1) and its activating
kinase (AtSnAK) determines their catalytic activities.";
J. Biol. Chem. 285:12071-12077(2010).
-!- FUNCTION: Catalytic subunit of the probable trimeric SNF1-related
protein kinase (SnRK) complex, which may play a role in a signal
transduction cascade regulating gene expression and carbohydrate
metabolism in higher plants. The SnRK complex may also be involved
in the regulation of fatty acid synthesis by phosphorylation of
acetyl-CoA carboxylase and in assimilation of nitrogen by
phosphorylating nitrate reductase. In vitro, KIN10 exhibits kinase
activity on sucrose phosphate synthase and the kinase activity is
inhibited by PRL1. May be a subunit of a SCF ubiquitin ligase
complex and thus be involved in proteasomal ubiquitination.
Phosphorylates GRIK1/SNAK2 and GRIK2/SNAK1 in vitro.
{ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:11387208,
ECO:0000269|PubMed:20164192}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by phosphorylation at Thr-198.
{ECO:0000269|PubMed:19339507}.
-!- SUBUNIT: Subunit of a probable heterotrimeric complex consisting
of an alpha catalytic (KIN10 or KIN11) subunit, and a beta (KINB)
and a gamma (KING or SNF4) non-catalytic regulatory subunits.
Interacts with KINB2, KINB3, SNF4 and probably with KINB1 and
KING1. Interacts with SKP1/ASK1, PAD1, the N-terminus of PRL1 and
the WD40 domain of 5PTase13. Potential subunit of a SCF ubiquitin
ligase complex consisting of a SNF1-related protein kinase, SKP1
and CUL1. The association of the SCF complex with the proteasome
may be mediated by PAD1 and seems to be inhibited by the
interaction with PRL1. Interacts with DSP4.
{ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:10929106,
ECO:0000269|PubMed:11387208, ECO:0000269|PubMed:11522840,
ECO:0000269|PubMed:15803412, ECO:0000269|PubMed:18931139}.
-!- INTERACTION:
Q93V58:GRIK1; NbExp=2; IntAct=EBI-2107143, EBI-6399184;
Q5HZ38:GRIK2; NbExp=2; IntAct=EBI-2107143, EBI-6399237;
Q9SCY5:KINB2; NbExp=3; IntAct=EBI-2107143, EBI-2042436;
Q42384:PRL1; NbExp=3; IntAct=EBI-2107143, EBI-1382964;
Q944A6:SNF4; NbExp=2; IntAct=EBI-2107143, EBI-2360649;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q38997-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q38997-2; Sequence=VSP_009001;
-!- INDUCTION: Induced by sucrose. {ECO:0000269|PubMed:10220464}.
-!- PTM: Autophosphorylated. Phosphorylated at Thr-198 by GRIK1/SNAK2
and GRIK2/SNAK1. {ECO:0000269|PubMed:10220464,
ECO:0000269|PubMed:19339507}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
URL="http://plantsp.genomics.purdue.edu/family/class.html";
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EMBL; M93023; AAA32736.1; -; Genomic_DNA.
EMBL; X94757; CAA64384.1; -; mRNA.
EMBL; DQ778957; ABH11527.1; -; mRNA.
EMBL; AC008261; AAF26165.1; -; Genomic_DNA.
EMBL; CP002686; AEE73607.1; -; Genomic_DNA.
EMBL; CP002686; AEE73608.1; -; Genomic_DNA.
EMBL; CP002686; AEE73609.1; -; Genomic_DNA.
EMBL; AY093170; AAM13169.1; -; mRNA.
EMBL; BT010386; AAQ56829.1; -; mRNA.
EMBL; X79707; CAA56146.1; -; Genomic_DNA.
EMBL; X86966; CAA60529.1; -; Genomic_DNA.
PIR; JC1446; JC1446.
RefSeq; NP_001118546.1; NM_001125074.2. [Q38997-2]
RefSeq; NP_566130.1; NM_110974.5. [Q38997-2]
RefSeq; NP_850488.1; NM_180157.1. [Q38997-1]
UniGene; At.22965; -.
ProteinModelPortal; Q38997; -.
SMR; Q38997; -.
BioGrid; 6592; 36.
IntAct; Q38997; 9.
STRING; 3702.AT3G01090.2; -.
iPTMnet; Q38997; -.
PaxDb; Q38997; -.
PRIDE; Q38997; -.
EnsemblPlants; AT3G01090.1; AT3G01090.1; AT3G01090. [Q38997-2]
EnsemblPlants; AT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
EnsemblPlants; AT3G01090.3; AT3G01090.3; AT3G01090. [Q38997-2]
GeneID; 821259; -.
Gramene; AT3G01090.1; AT3G01090.1; AT3G01090. [Q38997-2]
Gramene; AT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
Gramene; AT3G01090.3; AT3G01090.3; AT3G01090. [Q38997-2]
KEGG; ath:AT3G01090; -.
Araport; AT3G01090; -.
TAIR; locus:2102132; AT3G01090.
eggNOG; KOG0583; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000233016; -.
InParanoid; Q38997; -.
KO; K07198; -.
OMA; QGVRRAK; -.
OrthoDB; EOG0936066G; -.
PhylomeDB; Q38997; -.
BRENDA; 2.7.11.1; 399.
Reactome; R-ATH-163680; AMPK inhibits chREBP transcriptional activation activity.
Reactome; R-ATH-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-ATH-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
PRO; PR:Q38997; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q38997; baseline and differential.
Genevisible; Q38997; AT.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
GO; GO:0009594; P:detection of nutrient; IDA:TAIR.
GO; GO:0003006; P:developmental process involved in reproduction; IMP:TAIR.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0010150; P:leaf senescence; IMP:TAIR.
GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
GO; GO:0080022; P:primary root development; IMP:TAIR.
GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
GO; GO:0010050; P:vegetative phase change; IMP:TAIR.
InterPro; IPR028375; KA1/Ssp2_C.
InterPro; IPR001772; KA1_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR015940; UBA.
InterPro; IPR009060; UBA-like_sf.
Pfam; PF02149; KA1; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00627; UBA; 1.
SMART; SM00220; S_TKc; 1.
SMART; SM00165; UBA; 1.
SUPFAM; SSF103243; SSF103243; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50032; KA1; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS50030; UBA; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Carbohydrate metabolism;
Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism;
Isopeptide bond; Kinase; Lipid biosynthesis; Lipid metabolism;
Nitrate assimilation; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 535 SNF1-related protein kinase catalytic
subunit alpha KIN10.
/FTId=PRO_0000086128.
DOMAIN 42 294 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 315 355 UBA. {ECO:0000255|PROSITE-
ProRule:PRU00212}.
DOMAIN 486 534 KA1. {ECO:0000255|PROSITE-
ProRule:PRU00565}.
NP_BIND 48 56 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 165 165 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 71 71 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000250|UniProtKB:Q93V58}.
MOD_RES 198 198 Phosphothreonine; by GRIK1 or GRIK2.
{ECO:0000269|PubMed:19339507}.
CROSSLNK 43 43 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:17272265}.
VAR_SEQ 1 23 Missing (in isoform 2).
{ECO:0000303|Ref.2, ECO:0000303|Ref.3}.
/FTId=VSP_009001.
MUTAGEN 198 198 T->A: Abolishes phosphorylation by GRIK1
or GRIK2 leading to inactivation of the
protein. {ECO:0000269|PubMed:19339507,
ECO:0000269|PubMed:20164192}.
SEQUENCE 535 AA; 61182 MW; FFFC383223FD8317 CRC64;
MFKRVDEFNL VSSTIDHRIF KSRMDGSGTG SRSGVESILP NYKLGRTLGI GSFGRVKIAE
HALTGHKVAI KILNRRKIKN MEMEEKVRRE IKILRLFMHP HIIRLYEVIE TPTDIYLVME
YVNSGELFDY IVEKGRLQED EARNFFQQII SGVEYCHRNM VVHRDLKPEN LLLDSKCNVK
IADFGLSNIM RDGHFLKTSC GSPNYAAPEV ISGKLYAGPE VDVWSCGVIL YALLCGTLPF
DDENIPNLFK KIKGGIYTLP SHLSPGARDL IPRMLVVDPM KRVTIPEIRQ HPWFQAHLPR
YLAVPPPDTV QQAKKIDEEI LQEVINMGFD RNHLIESLRN RTQNDGTVTY YLILDNRFRA
SSGYLGAEFQ ETMEGTPRMH PAESVASPVS HRLPGLMEYQ GVGLRSQYPV ERKWALGLQS
RAHPREIMTE VLKALQDLNV CWKKIGHYNM KCRWVPNSSA DGMLSNSMHD NNYFGDESSI
IENEAAVKSP NVVKFEIQLY KTRDDKYLLD LQRVQGPQFL FLDLCAAFLA QLRVL


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U1918p CLIA kit cAMP-dependent protein kinase catalytic subunit alpha,Pig,PKA C-alpha,PRKACA,Sus scrofa 96T
U1918p CLIA cAMP-dependent protein kinase catalytic subunit alpha,Pig,PKA C-alpha,PRKACA,Sus scrofa 96T
E1918p ELISA cAMP-dependent protein kinase catalytic subunit alpha,Pig,PKA C-alpha,PRKACA,Sus scrofa 96T
EIAAB31922 Calmodulin-dependent calcineurin A subunit alpha isoform,CALNA,CAM-PRP catalytic subunit,CNA,Homo sapiens,Human,PPP3CA,Serine_threonine-protein phosphatase 2B catalytic subunit alpha isoform
EIAAB31921 Calmodulin-dependent calcineurin A subunit alpha isoform,Calna,CAM-PRP catalytic subunit,Ppp3ca,Rat,Rattus norvegicus,Serine_threonine-protein phosphatase 2B catalytic subunit alpha isoform
EIAAB31920 Calmodulin-dependent calcineurin A subunit alpha isoform,Calna,CAM-PRP catalytic subunit,Mouse,Mus musculus,Ppp3ca,Serine_threonine-protein phosphatase 2B catalytic subunit alpha isoform
E1918b ELISA kit Bos taurus,Bovine,cAMP-dependent protein kinase catalytic subunit alpha,PKA C-alpha,PRKACA 96T


 

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