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Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PP2A subunit B isoform B55-alpha) (PP2A subunit B isoform PR55-alpha) (PP2A subunit B isoform R2-alpha) (PP2A subunit B isoform alpha)

 2ABA_HUMAN              Reviewed;         447 AA.
P63151; B2RBU8; B4E1T7; P50409; Q00007;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
27-SEP-2004, sequence version 1.
05-DEC-2018, entry version 153.
RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;
AltName: Full=PP2A subunit B isoform B55-alpha;
AltName: Full=PP2A subunit B isoform PR55-alpha;
AltName: Full=PP2A subunit B isoform R2-alpha;
AltName: Full=PP2A subunit B isoform alpha;
Name=PPP2R2A;
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), AND TISSUE SPECIFICITY.
TISSUE=Lung fibroblast;
PubMed=1849734; DOI=10.1021/bi00229a001;
Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J.,
Merlevede W., Hofsteenge J., Hemmings B.A.;
"Structure of the 55-kDa regulatory subunit of protein phosphatase 2A:
evidence for a neuronal-specific isoform.";
Biochemistry 30:3589-3597(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Trachea;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Blood;
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).
[6]
INTERACTION WITH TP53.
PubMed=17245430; DOI=10.1038/sj.emboj.7601519;
Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.;
"A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-
induced dephosphorylation of p53 at Thr55.";
EMBO J. 26:402-411(2007).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[10]
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).
[11]
INTERACTION WITH IER5.
PubMed=25816751; DOI=10.1016/j.febslet.2015.03.019;
Ishikawa Y., Kawabata S., Sakurai H.;
"HSF1 transcriptional activity is modulated by IER5 and PP2A/B55.";
FEBS Lett. 589:1150-1155(2015).
[12]
INTERACTION WITH FAM122A.
PubMed=27588481; DOI=10.18632/oncotarget.11698;
Fan L., Liu M.H., Guo M., Hu C.X., Yan Z.W., Chen J., Chen G.Q.,
Huang Y.;
"FAM122A, a new endogenous inhibitor of protein phosphatase 2A.";
Oncotarget 7:63887-63900(2016).
[13]
INTERACTION WITH MFHAS1.
PubMed=28609714; DOI=10.1016/j.molimm.2017.06.017;
Shi Q., Xiong B., Zhong J., Wang H., Ma D., Miao C.;
"MFHAS1 suppresses TLR4 signaling pathway via induction of PP2A C
subunit cytoplasm translocation and inhibition of c-Jun
dephosphorylation at Thr239.";
Mol. Immunol. 88:79-88(2017).
-!- FUNCTION: The B regulatory subunit might modulate substrate
selectivity and catalytic activity, and also might direct the
localization of the catalytic enzyme to a particular subcellular
compartment.
-!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A,
PPP2R2A, PPP2R5E and TBCD (By similarity). PP2A consists of a
common heterodimeric core enzyme, composed of a 36 kDa catalytic
subunit (subunit C) and a 65 kDa constant regulatory subunit (PR65
or subunit A), that associates with a variety of regulatory
subunits. Proteins that associate with the core dimer include
three families of regulatory subunits B (the R2/B/PR55/B55,
R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa
variable regulatory subunit, viral proteins, and cell signaling
molecules (By similarity). Interacts with TP53 (PubMed:17245430).
Interacts with IER5 (PubMed:25816751). Interacts with MFHAS1; the
interaction is direct (PubMed:28609714). Interacts with FAM122A
(PubMed:27588481). {ECO:0000250, ECO:0000269|PubMed:17245430,
ECO:0000269|PubMed:25816751, ECO:0000269|PubMed:27588481,
ECO:0000269|PubMed:28609714}.
-!- INTERACTION:
P30153:PPP2R1A; NbExp=17; IntAct=EBI-1048931, EBI-302388;
P30154:PPP2R1B; NbExp=5; IntAct=EBI-1048931, EBI-357094;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P63151-1; Sequence=Displayed;
Name=2;
IsoId=P63151-2; Sequence=VSP_043100;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined.
{ECO:0000269|PubMed:1849734}.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B
family. {ECO:0000305}.
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EMBL; M64929; AAA36490.1; -; mRNA.
EMBL; AK303981; BAG64899.1; -; mRNA.
EMBL; AK314823; BAG37345.1; -; mRNA.
EMBL; AC022911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471080; EAW63578.1; -; Genomic_DNA.
EMBL; BC041071; AAH41071.1; -; mRNA.
CCDS; CCDS34867.1; -. [P63151-1]
CCDS; CCDS55213.1; -. [P63151-2]
PIR; A38351; A38351.
RefSeq; NP_001171062.1; NM_001177591.1. [P63151-2]
RefSeq; NP_002708.1; NM_002717.3. [P63151-1]
UniGene; Hs.146339; -.
PDB; 3DW8; X-ray; 2.85 A; B/E=1-447.
PDBsum; 3DW8; -.
ProteinModelPortal; P63151; -.
SMR; P63151; -.
BioGrid; 111512; 125.
CORUM; P63151; -.
DIP; DIP-29398N; -.
IntAct; P63151; 65.
MINT; P63151; -.
STRING; 9606.ENSP00000325074; -.
BindingDB; P63151; -.
ChEMBL; CHEMBL4284; -.
iPTMnet; P63151; -.
PhosphoSitePlus; P63151; -.
SwissPalm; P63151; -.
BioMuta; PPP2R2A; -.
DMDM; 52783535; -.
EPD; P63151; -.
MaxQB; P63151; -.
PaxDb; P63151; -.
PeptideAtlas; P63151; -.
PRIDE; P63151; -.
DNASU; 5520; -.
Ensembl; ENST00000315985; ENSP00000325074; ENSG00000221914. [P63151-2]
Ensembl; ENST00000380737; ENSP00000370113; ENSG00000221914. [P63151-1]
GeneID; 5520; -.
KEGG; hsa:5520; -.
UCSC; uc003xeu.4; human. [P63151-1]
CTD; 5520; -.
DisGeNET; 5520; -.
EuPathDB; HostDB:ENSG00000221914.8; -.
GeneCards; PPP2R2A; -.
HGNC; HGNC:9304; PPP2R2A.
HPA; CAB079289; -.
HPA; HPA042122; -.
HPA; HPA042770; -.
MIM; 604941; gene.
neXtProt; NX_P63151; -.
OpenTargets; ENSG00000221914; -.
PharmGKB; PA33668; -.
eggNOG; KOG1354; Eukaryota.
eggNOG; COG5170; LUCA.
GeneTree; ENSGT00940000153436; -.
HOGENOM; HOG000089745; -.
HOVERGEN; HBG000012; -.
InParanoid; P63151; -.
KO; K04354; -.
OMA; PGGCTSL; -.
OrthoDB; EOG091G09BB; -.
PhylomeDB; P63151; -.
TreeFam; TF105553; -.
Reactome; R-HSA-2995383; Initiation of Nuclear Envelope Reformation.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
SignaLink; P63151; -.
SIGNOR; P63151; -.
ChiTaRS; PPP2R2A; human.
EvolutionaryTrace; P63151; -.
GeneWiki; PPP2R2A; -.
GenomeRNAi; 5520; -.
PRO; PR:P63151; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000221914; Expressed in 236 organ(s), highest expression level in corpus callosum.
CleanEx; HS_PPP2R2A; -.
ExpressionAtlas; P63151; baseline and differential.
Genevisible; P63151; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB.
GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
GO; GO:0019888; F:protein phosphatase regulator activity; TAS:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; IBA:GO_Central.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR000009; PP2A_PR55.
InterPro; IPR018067; PP2A_PR55_CS.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR11871; PTHR11871; 1.
PIRSF; PIRSF037309; PP2A_PR55; 1.
PRINTS; PR00600; PP2APR55.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS01024; PR55_1; 1.
PROSITE; PS01025; PR55_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Reference proteome; Repeat; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 447 Serine/threonine-protein phosphatase 2A
55 kDa regulatory subunit B alpha
isoform.
/FTId=PRO_0000071415.
REPEAT 26 65 WD 1.
REPEAT 91 132 WD 2.
REPEAT 175 213 WD 3.
REPEAT 224 264 WD 4.
REPEAT 283 321 WD 5.
REPEAT 338 379 WD 6.
REPEAT 414 446 WD 7.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
VAR_SEQ 1 2 MA -> MFPKFSLRSMFH (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043100.
STRAND 13 16 {ECO:0000244|PDB:3DW8}.
STRAND 21 23 {ECO:0000244|PDB:3DW8}.
HELIX 27 29 {ECO:0000244|PDB:3DW8}.
STRAND 30 36 {ECO:0000244|PDB:3DW8}.
STRAND 38 47 {ECO:0000244|PDB:3DW8}.
STRAND 50 57 {ECO:0000244|PDB:3DW8}.
STRAND 71 78 {ECO:0000244|PDB:3DW8}.
STRAND 83 85 {ECO:0000244|PDB:3DW8}.
HELIX 86 88 {ECO:0000244|PDB:3DW8}.
STRAND 90 92 {ECO:0000244|PDB:3DW8}.
STRAND 98 101 {ECO:0000244|PDB:3DW8}.
STRAND 106 114 {ECO:0000244|PDB:3DW8}.
STRAND 119 132 {ECO:0000244|PDB:3DW8}.
STRAND 156 172 {ECO:0000244|PDB:3DW8}.
STRAND 182 185 {ECO:0000244|PDB:3DW8}.
STRAND 189 195 {ECO:0000244|PDB:3DW8}.
STRAND 197 204 {ECO:0000244|PDB:3DW8}.
STRAND 207 216 {ECO:0000244|PDB:3DW8}.
HELIX 222 224 {ECO:0000244|PDB:3DW8}.
STRAND 229 234 {ECO:0000244|PDB:3DW8}.
STRAND 241 246 {ECO:0000244|PDB:3DW8}.
STRAND 251 255 {ECO:0000244|PDB:3DW8}.
TURN 256 258 {ECO:0000244|PDB:3DW8}.
STRAND 260 262 {ECO:0000244|PDB:3DW8}.
STRAND 267 269 {ECO:0000244|PDB:3DW8}.
HELIX 280 284 {ECO:0000244|PDB:3DW8}.
STRAND 288 293 {ECO:0000244|PDB:3DW8}.
STRAND 297 312 {ECO:0000244|PDB:3DW8}.
STRAND 323 325 {ECO:0000244|PDB:3DW8}.
HELIX 327 329 {ECO:0000244|PDB:3DW8}.
TURN 330 332 {ECO:0000244|PDB:3DW8}.
HELIX 333 338 {ECO:0000244|PDB:3DW8}.
HELIX 341 343 {ECO:0000244|PDB:3DW8}.
STRAND 348 350 {ECO:0000244|PDB:3DW8}.
STRAND 354 360 {ECO:0000244|PDB:3DW8}.
STRAND 365 370 {ECO:0000244|PDB:3DW8}.
TURN 371 373 {ECO:0000244|PDB:3DW8}.
STRAND 376 380 {ECO:0000244|PDB:3DW8}.
HELIX 410 412 {ECO:0000244|PDB:3DW8}.
STRAND 421 424 {ECO:0000244|PDB:3DW8}.
STRAND 426 434 {ECO:0000244|PDB:3DW8}.
STRAND 439 443 {ECO:0000244|PDB:3DW8}.
SEQUENCE 447 AA; 51692 MW; F4D407FF7ADA4ED6 CRC64;
MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE
NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK
LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI
NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN
TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM
MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG
SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL
HTAWHPKENI IAVATTNNLY IFQDKVN


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E1056r Pig ELISA Kit FOR Serine per threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform 96T
E14916h Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform 96T
H0417 Serine threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PPP2R2A), Rat, ELISA Kit 96T
H0415 Serine threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PPP2R2A), Pig, ELISA Kit 96T
H0435 Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PPP2R1A), Pig, ELISA Kit 96T
E13952b Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform 96T
GWB-7124AE PROTEIN PHOSPHATASE PP2A 65 KD REGULATORY SUBUNIT BETA ISOFORM (PPP2R1B) Rabbit anti-Rat Polyclonal (aa7-19) Antibody
H0434 Serine threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (PPP2R1A), Mouse, ELISA Kit 96T
CSB-EL018562HU Human Serine per threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform(PPP2R1A) ELISA kit 96T
H0416 Serine threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform (PPP2R2A), Rabbit, ELISA Kit 96T


 

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