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Inhibitor of growth protein 2 (Inhibitor of growth 1-like protein) (ING1Lp) (p32) (p33ING2)

 ING2_HUMAN              Reviewed;         280 AA.
Q9H160; B6ZDS1; O95698;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=Inhibitor of growth protein 2;
AltName: Full=Inhibitor of growth 1-like protein;
Short=ING1Lp;
AltName: Full=p32;
AltName: Full=p33ING2;
Name=ING2; Synonyms=ING1L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM ING2A), AND TISSUE
SPECIFICITY.
PubMed=10072587;
Shimada Y., Saito A., Suzuki M., Takahashi E., Horie M.;
"Cloning of a novel gene (ING1L) homologous to ING1, a candidate tumor
suppressor.";
Cytogenet. Cell Genet. 83:232-235(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2A), FUNCTION, AND INDUCTION.
PubMed=11481424; DOI=10.1073/pnas.161151798;
Nagashima M., Shiseki M., Miura K., Hagiwara K., Linke S.P.,
Pedeux R., Wang X.W., Yokota J., Riabowol K., Harris C.C.;
"DNA damage-inducible gene p33ING2 negatively regulates cell
proliferation through acetylation of p53.";
Proc. Natl. Acad. Sci. U.S.A. 98:9671-9676(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2B), AND ALTERNATIVE SPLICING.
PubMed=18951897; DOI=10.1016/j.febslet.2008.10.024;
Unoki M., Kumamoto K., Robles A.I., Shen J.C., Zheng Z.-M.,
Harris C.C.;
"A novel ING2 isoform, ING2b, synergizes with ING2a to prevent cell
cycle arrest and apoptosis.";
FEBS Lett. 582:3868-3874(2008).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ING2A).
TISSUE=Mammary tumor;
Cal S., Freije J.M., Lopez-Otin C.;
"ING2, a new possible gene suppressor tumor.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ING2B).
TISSUE=Amygdala;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ING2A).
TISSUE=Lung;
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).
[8]
PROTEIN SEQUENCE OF 23-44, IDENTIFICATION IN MSIN3A-LIKE COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11784859; DOI=10.1128/MCB.22.3.835-848.2002;
Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.;
"Role of the Sin3-histone deacetylase complex in growth regulation by
the candidate tumor suppressor p33(ING1).";
Mol. Cell. Biol. 22:835-848(2002).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12859901; DOI=10.1016/S0092-8674(03)00480-X;
Gozani O., Karuman P., Jones D.R., Ivanov D., Cha J., Lugovskoy A.A.,
Baird C.L., Zhu H., Field S.J., Lessnick S.L., Villasenor J.,
Mehrotra B., Chen J., Rao V.R., Brugge J.S., Ferguson C.G.,
Payrastre B., Myszka D.G., Cantley L.C., Wagner G., Divecha N.,
Prestwich G.D., Yuan J.;
"The PHD finger of the chromatin-associated protein ING2 functions as
a nuclear phosphoinositide receptor.";
Cell 114:99-111(2003).
[10]
PHOSPHOINOSITIDE-BINDING.
PubMed=16893883; DOI=10.1074/jbc.M605624200;
Kaadige M.R., Ayer D.E.;
"The polybasic region that follows the plant homeodomain zinc finger 1
of Pf1 is necessary and sufficient for specific phosphoinositide
binding.";
J. Biol. Chem. 281:28831-28836(2006).
[11]
IDENTIFICATION IN MSIN3A COMPLEX.
PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007;
Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W.,
Lane W.S., Tan S., Yang X.-J., Cote J.;
"ING tumor suppressor proteins are critical regulators of chromatin
acetylation required for genome expression and perpetuation.";
Mol. Cell 21:51-64(2006).
[12]
DOMAIN PHD-TYPE ZINC-FINGER, AND INTERACTION WITH HISTONES H3K4ME3 AND
H3K4ME2.
PubMed=16728974; DOI=10.1038/nature04835;
Shi X., Hong T., Walter K.L., Ewalt M., Michishita E., Hung T.,
Carney D., Pena P., Lan F., Kaadige M.R., Lacoste N., Cayrou C.,
Davrazou F., Saha A., Cairns B.R., Ayer D.E., Kutateladze T.G.,
Shi Y., Cote J., Chua K.F., Gozani O.;
"ING2 PHD domain links histone H3 lysine 4 methylation to active gene
repression.";
Nature 442:96-99(2006).
[13]
SUMOYLATION AT LYS-195.
PubMed=20676127; DOI=10.1038/onc.2010.325;
Ythier D., Larrieu D., Binet R., Binda O., Brambilla C., Gazzeri S.,
Pedeux R.;
"Sumoylation of ING2 regulates the transcription mediated by Sin3A.";
Oncogene 29:5946-5956(2010).
-!- FUNCTION: Seems to be involved in p53/TP53 activation and
p53/TP53-dependent apoptotic pathways, probably by enhancing
acetylation of p53/TP53. Component of a mSin3A-like corepressor
complex, which is probably involved in deacetylation of
nucleosomal histones. ING2 activity seems to be modulated by
binding to phosphoinositides (PtdInsPs).
{ECO:0000269|PubMed:11481424, ECO:0000269|PubMed:12859901}.
-!- SUBUNIT: Interacts with H3K4me3 and to a lesser extent with
H3K4me2. Component of a mSin3A-like complex at least consisting of
SIN3A, HDAC1, HDAC2, RBBP4/RbAp48, RBBP7/RbAp46, SAP30 and ING2.
{ECO:0000269|PubMed:11784859, ECO:0000269|PubMed:16387653,
ECO:0000269|PubMed:16728974}.
-!- INTERACTION:
P12004:PCNA; NbExp=3; IntAct=EBI-389787, EBI-358311;
Q9HCE7-2:SMURF1; NbExp=3; IntAct=EBI-389787, EBI-9845742;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12859901}.
Note=Predominantly nuclear. Localized to chromatin and nuclear
matrix. Upon reduced PtdIns(5)P levels seems to be released from
chromatin and, at least partially, translocated to the cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=ING2a;
IsoId=Q9H160-1; Sequence=Displayed;
Name=ING2b;
IsoId=Q9H160-2; Sequence=VSP_047821;
Note=Low expression except in testis, where it reaches half of
ING2a levels.;
-!- TISSUE SPECIFICITY: Widely expressed. Higher expressed in colon-
cancer tumor than in normal colon tissues.
{ECO:0000269|PubMed:10072587}.
-!- INDUCTION: Induced by the DNA-damaging agents etoposide and
neocarzinostatin. {ECO:0000269|PubMed:11481424}.
-!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
{ECO:0000269|PubMed:16728974}.
-!- DOMAIN: The polybasic region (PBR) is responsive to the binding to
phosphoinositides (PtdInsPs), including phosphatidylinositol 5-
phosphate (PtdIns(5)P). {ECO:0000269|PubMed:16728974}.
-!- PTM: Sumoylation enhances its association with SIN3A and is
required for binding to some target gene promoters, this is the
case for TMEM71. {ECO:0000269|PubMed:20676127}.
-!- SIMILARITY: Belongs to the ING family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ING2ID40975ch4q35.html";
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EMBL; AB012853; BAA36419.1; -; mRNA.
EMBL; AF053537; AAG11395.1; -; mRNA.
EMBL; AF062748; AAG11396.1; -; Genomic_DNA.
EMBL; AF062747; AAG11396.1; JOINED; Genomic_DNA.
EMBL; AB196793; BAF30476.1; -; mRNA.
EMBL; AJ006851; CAC20567.1; -; mRNA.
EMBL; AK294310; BAH11731.1; -; mRNA.
EMBL; AC107214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030128; AAH30128.1; -; mRNA.
CCDS; CCDS3833.1; -. [Q9H160-1]
RefSeq; NP_001278888.1; NM_001291959.1. [Q9H160-2]
RefSeq; NP_001555.1; NM_001564.3. [Q9H160-1]
UniGene; Hs.107153; -.
ProteinModelPortal; Q9H160; -.
SMR; Q9H160; -.
BioGrid; 109834; 47.
CORUM; Q9H160; -.
IntAct; Q9H160; 12.
MINT; MINT-2830779; -.
STRING; 9606.ENSP00000307183; -.
ChEMBL; CHEMBL3784904; -.
iPTMnet; Q9H160; -.
PhosphoSitePlus; Q9H160; -.
BioMuta; ING2; -.
DMDM; 59798471; -.
EPD; Q9H160; -.
MaxQB; Q9H160; -.
PaxDb; Q9H160; -.
PeptideAtlas; Q9H160; -.
PRIDE; Q9H160; -.
DNASU; 3622; -.
Ensembl; ENST00000302327; ENSP00000307183; ENSG00000168556. [Q9H160-1]
GeneID; 3622; -.
KEGG; hsa:3622; -.
UCSC; uc003ivs.2; human. [Q9H160-1]
CTD; 3622; -.
DisGeNET; 3622; -.
EuPathDB; HostDB:ENSG00000168556.6; -.
GeneCards; ING2; -.
HGNC; HGNC:6063; ING2.
HPA; HPA019486; -.
HPA; HPA021517; -.
MIM; 604215; gene.
neXtProt; NX_Q9H160; -.
OpenTargets; ENSG00000168556; -.
PharmGKB; PA29873; -.
eggNOG; KOG1973; Eukaryota.
eggNOG; COG5034; LUCA.
GeneTree; ENSGT00550000074538; -.
HOGENOM; HOG000239724; -.
HOVERGEN; HBG006607; -.
InParanoid; Q9H160; -.
KO; K19198; -.
OMA; LCHMTNG; -.
OrthoDB; EOG091G0J8Y; -.
PhylomeDB; Q9H160; -.
TreeFam; TF352014; -.
Reactome; R-HSA-6811555; PI5P Regulates TP53 Acetylation.
SIGNOR; Q9H160; -.
ChiTaRS; ING2; human.
GeneWiki; ING2; -.
GenomeRNAi; 3622; -.
PRO; PR:Q9H160; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000168556; -.
CleanEx; HS_ING2; -.
ExpressionAtlas; Q9H160; baseline and differential.
Genevisible; Q9H160; HS.
GO; GO:0016602; C:CCAAT-binding factor complex; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0030317; P:flagellated sperm motility; ISS:BHF-UCL.
GO; GO:0048133; P:male germ-line stem cell asymmetric division; ISS:BHF-UCL.
GO; GO:0007141; P:male meiosis I; ISS:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:InterPro.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; TAS:BHF-UCL.
GO; GO:0031065; P:positive regulation of histone deacetylation; ISS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:2000772; P:regulation of cellular senescence; NAS:BHF-UCL.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; NAS:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0072520; P:seminiferous tubule development; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007286; P:spermatid development; ISS:BHF-UCL.
GO; GO:0007283; P:spermatogenesis; ISS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR028639; ING2.
InterPro; IPR024610; ING_N_histone_binding.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR10333:SF37; PTHR10333:SF37; 1.
Pfam; PF12998; ING; 1.
SMART; SM01408; ING; 1.
SMART; SM00249; PHD; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Direct protein sequencing; Growth regulation;
Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 280 Inhibitor of growth protein 2.
/FTId=PRO_0000212663.
ZN_FING 212 261 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
REGION 264 280 PBR. {ECO:0000269|PubMed:16728974}.
COILED 48 120 {ECO:0000255}.
METAL 215 215 Zinc 1. {ECO:0000250|UniProtKB:Q9UK53}.
METAL 217 217 Zinc 1. {ECO:0000250|UniProtKB:Q9UK53}.
METAL 228 228 Zinc 2. {ECO:0000250|UniProtKB:Q9UK53}.
METAL 233 233 Zinc 2. {ECO:0000250|UniProtKB:Q9UK53}.
METAL 239 239 Zinc 1; via pros nitrogen.
{ECO:0000250|UniProtKB:Q9UK53}.
METAL 242 242 Zinc 1. {ECO:0000250|UniProtKB:Q9UK53}.
METAL 255 255 Zinc 2. {ECO:0000250|UniProtKB:Q9UK53}.
METAL 258 258 Zinc 2. {ECO:0000250|UniProtKB:Q9UK53}.
BINDING 214 214 Histone H3K4me3.
{ECO:0000250|UniProtKB:Q9UK53}.
BINDING 225 225 Histone H3K4me3.
{ECO:0000250|UniProtKB:Q9UK53}.
BINDING 229 229 Histone H3K4me3.
{ECO:0000250|UniProtKB:Q9UK53}.
BINDING 237 237 Histone H3K4me3.
{ECO:0000250|UniProtKB:Q9UK53}.
CROSSLNK 195 195 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000269|PubMed:20676127}.
VAR_SEQ 1 58 MLGQQQQQLYSSAALLTGERSRLLTCYVQDYLECVESLPHD
MQRNVSVLRELDNKYQE -> MDQDGDQQLGPSRILAPQ
(in isoform ING2b).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18951897}.
/FTId=VSP_047821.
CONFLICT 21 21 S -> T (in Ref. 4; CAC20567).
{ECO:0000305}.
SEQUENCE 280 AA; 32808 MW; DC85A6ECAF7A5D81 CRC64;
MLGQQQQQLY SSAALLTGER SRLLTCYVQD YLECVESLPH DMQRNVSVLR ELDNKYQETL
KEIDDVYEKY KKEDDLNQKK RLQQLLQRAL INSQELGDEK IQIVTQMLEL VENRARQMEL
HSQCFQDPAE SERASDKAKM DSSQPERSSR RPRRQRTSES RDLCHMANGI EDCDDQPPKE
KKSKSAKKKK RSKAKQEREA SPVEFAIDPN EPTYCLCNQV SYGEMIGCDN EQCPIEWFHF
SCVSLTYKPK GKWYCPKCRG DNEKTMDKST EKTKKDRRSR


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10-288-23152 Transforming Growth Factor beta 2 (Human). E coli - Glioblastoma-derived T-cell suppressor factor; BSC-1 cell growth inhibitor; Polyergin; Cetermin; TGFB2 protein; Transforming growth factor beta-2; T 0.05 mg
10-288-23152 Transforming Growth Factor beta 2 (Human). E coli - Glioblastoma-derived T-cell suppressor factor; BSC-1 cell growth inhibitor; Polyergin; Cetermin; TGFB2 protein; Transforming growth factor beta-2; T 0.005 mg
TM 1506 SOYA CASEIN DIGEST AGAR WITH INHIBITOR (a general purpose medium with inhibitor that inhibit the growth of Staphylococci.) 500 gm
CSB-EL011716MO Mouse Inhibitor of growth protein 5(ING5) ELISA kit 96T


 

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