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Mothers Against Decapentaplegic Homolog 2 (SMAD2) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS719384

Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that… More details

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Product Overview

Online Datasheet in PDF
Product Name
Mothers against decapentaplegic homolog 2 (SMAD2), Recombinant Protein
Full Product Name
Recombinant Human Mothers against decapentaplegic homolog 2 protein
Product Gene Name
Product Synonym Gene Name
MADH2; MADR2
Product Synonym Names
JV18-1; Mad-related protein 2; hMAD-2; SMAD family member 2; SMAD 2; Smad2; hSMAD2
Sequence
SSILPFTPPV VKRLLGWKKS AGGSGGAGGG EQNGQEEKWC EKAVKSLVKK LKKTGRLDEL EKAITTQNCN TKCVTIPSTC SEIWGLSTPN TIDQWDTTGL YSFSEQTRSL DGRLQVSHRK GLPHVIYCRL WRWPDLHSHH ELKAIENCEY AFNLKKDEVC VNPYHYQRVE TPVLPPVLVP RHTEILTELP PLDDYTHSIP ENTNFPAGIE PQSNYIPETP PPGYISEDGE TSDQQLNQSM DTGSPAELSP TTLSP
Host
E Coli
Form/Format
Liquid containing glycerol
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
56.2kD
Sequence Positions
2-467
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
601366
3D Structure
ModBase 3D Structure for Q15796

Product Categories/Family for SMAD2 recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for SMAD2 recombinant protein

Mad-related genes in the human.Riggins G.J., Thiagalingam S., Rosenblum E., Weinstein C.L., Kern S.E., Hamilton S.R., Willson J.K.V., Markowitz S.D., Kinzler K.W., Vogelstein B.V.Nat. Genet. 13:347-349(1996) Receptor-associated Mad homologues synergize as effectors of the TGF-beta response.Zhang Y., Feng X.-H., Wu R.-Y., Derynck R.Nature 383:168-172(1996) MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma.Eppert K., Scherer S.W., Ozcelik H., Pirone R., Hoodless P., Kim H., Tsui L.-C., Bapat B., Gallinger S., Andrulis I.L., Thomsen G.H., Wrana J.L., Attisano L.Cell 86:543-552(1996) Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible transcriptional complexes.Liu F., Pouponnot C., Massague J.Genes Dev. 11:3157-3167(1997) Characterization of the MADH2/Smad2 gene, a human Mad homolog responsible for the transforming growth factor-beta and activin signal transduction pathway.Takenoshita S., Mogi A., Nagashima M., Yang K., Yagi K., Hanyu A., Nagamachi Y., Miyazono K., Hagiwara K.Genomics 48:1-11(1998) Bienvenut W.V., von Kriegsheim A., Kolch W.Submitted (DEC-2008) to UniProtKB MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling.Macias-Silva M., Abdollah S., Hoodless P.A., Pirone R., Attisano L., Wrana J.L.Cell 87:1215-1224(1996) SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor.Tsukazaki T., Chiang T.A., Davison A.F., Attisano L., Wrana J.L.Cell 95:779-791(1998) Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors.Kawabata M., Inoue H., Hanyu A., Imamura T., Miyazono K.EMBO J. 17:4056-4065(1998) Alternatively spliced variant of Smad2 lacking exon 3. Comparison with wild-type Smad2 and Smad3.Yagi K., Goto D., Hamamoto T., Takenoshita S., Kato M., Miyazono K.J. Biol. Chem. 274:703-709(1999) The TGF-beta family mediator Smad1 is phosphorylated directly and activated functionally by the BMP receptor kinase.Kretzschmar M., Liu F., Hata A., Doody J., Massague J.Genes Dev. 11:984-995(1997) TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling.Abdollah S., Macias-Silva M., Tsukazaki T., Hayashi H., Attisano L., Wrana J.L.J. Biol. Chem. 272:27678-27685(1997) Characterization of human FAST-1, a TGF beta and activin signal transducer.Zhou S., Zawel L., Lengauer C., Kinzler K.W., Vogelstein B.Mol. Cell 2:121-127(1998) Roles of pathway-specific and inhibitory Smads in activin receptor signaling.Lebrun J.J., Takabe K., Chen Y., Vale W.Mol. Endocrinol. 13:15-23(1999) The adaptor molecule Disabled-2 links the transforming growth factor beta receptors to the Smad pathway.Hocevar B.A., Smine A., Xu X.X., Howe P.H.EMBO J. 20:2789-2801(2001) Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription.Leong G.M., Subramaniam N., Figueroa J., Flanagan J.L., Hayman M.J., Eisman J.A., Kouzmenko A.P.J. Biol. Chem. 276:18243-18248(2001) TGF-beta induces assembly of a Smad2-Smurf2 ubiquitin ligase complex that targets SnoN for degradation.Bonni S., Wang H.R., Causing C.G., Kavsak P., Stroschein S.L., Luo K., Wrana J.L.Nat. Cell Biol. 3:587-595(2001) Decorin suppresses transforming growth factor-beta-induced expression of plasminogen activator inhibitor-1 in human mesangial cells through a mechanism that involves Ca2+-dependent phosphorylation of Smad2 at serine-240.Abdel-Wahab N., Wicks S.J., Mason R.M., Chantry A.Biochem. J. 362:643-649(2002) Modulation of Smad2-mediated signaling by extracellular signal-regulated kinase.Funaba M., Zimmerman C.M., Mathews L.S.J. Biol. Chem. 277:41361-41368(2002) MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling.Lin F., Morrison J.M., Wu W., Worman H.J.Hum. Mol. Genet. 14:437-445(2005) The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines.Pan D., Estevez-Salmeron L.D., Stroschein S.L., Zhu X., He J., Zhou S., Luo K.J. Biol. Chem. 280:15992-16001(2005) Cloning and functional characterization of a new Ski homolog, Fussel-18, specifically expressed in neuronal tissues.Arndt S., Poser I., Schubert T., Moser M., Bosserhoff A.-K.Lab. Invest. 85:1330-1341(2005) PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling.Lin X., Duan X., Liang Y.Y., Su Y., Wrighton K.H., Long J., Hu M., Davis C.M., Wang J., Brunicardi F.C., Shi Y., Chen Y.G., Meng A., Feng X.H.Cell 125:915-928(2006) Hematopoiesis controlled by distinct TIF1gamma and Smad4 branches of the TGFbeta pathway.He W., Dorn D.C., Erdjument-Bromage H., Tempst P., Moore M.A., Massague J.Cell 125:929-941(2006) The DNA binding activities of Smad2 and Smad3 are regulated by coactivator-mediated acetylation.Simonsson M., Kanduri M., Gronroos E., Heldin C.H., Ericsson J.J. Biol. Chem. 281:39870-39880(2006) Potentiation of Smad-mediated transcriptional activation by the RNA-binding protein RBPMS.Sun Y., Ding L., Zhang H., Han J., Yang X., Yan J., Zhu Y., Li J., Song H., Ye Q.Nucleic Acids Res. 34:6314-6326(2006) 3-Phosphoinositide-dependent PDK1 negatively regulates transforming growth factor-beta-induced signaling in a kinase-dependent manner through physical interaction with Smad proteins.Seong H.A., Jung H., Kim K.T., Ha H.J. Biol. Chem. 282:12272-12289(2007) Fussel-15, a novel Ski/Sno homolog protein, antagonizes BMP signaling.Arndt S., Poser I., Moser M., Bosserhoff A.-K.Mol. Cell. Neurosci. 34:603-611(2007) Smad3 is acetylated by p300/CBP to regulate its transactivation activity.Inoue Y., Itoh Y., Abe K., Okamoto T., Daitoku H., Fukamizu A., Onozaki K., Hayashi H.Oncogene 26:500-508(2007) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008) TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal.Varelas X., Sakuma R., Samavarchi-Tehrani P., Peerani R., Rao B.M., Dembowy J., Yaffe M.B., Zandstra P.W., Wrana J.L.Nat. Cell Biol. 10:837-848(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling.Dai F., Lin X., Chang C., Feng X.H.Dev. Cell 16:345-357(2009) SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal in gastric cancer cells.Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M., Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M., Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., Imamura T.J. Biol. Chem. 284:3334-3344(2009) TMEPAI, a transmembrane TGF-beta-inducible protein, sequesters Smad proteins from active participation in TGF-beta signaling.Watanabe Y., Itoh S., Goto T., Ohnishi E., Inamitsu M., Itoh F., Satoh K., Wiercinska E., Yang W., Shi L., Tanaka A., Nakano N., Mommaas A.M., Shibuya H., Ten Dijke P., Kato M.Mol. Cell 37:123-134(2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) ZNF580, a novel C2H2 zinc-finger transcription factor, interacts with the TGF-beta signal molecule Smad2.Luo Y., Hu W., Xu R., Hou B., Zhang L., Zhang W.Cell Biol. Int. 35:1153-1157(2011) USP15 is a deubiquitylating enzyme for receptor-activated SMADs.Inui M., Manfrin A., Mamidi A., Martello G., Morsut L., Soligo S., Enzo E., Moro S., Polo S., Dupont S., Cordenonsi M., Piccolo S.Nat. Cell Biol. 13:1368-1375(2011) Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway.Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.Cell. Signal. 24:1999-2006(2012) Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration.Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.Mol. Cell 49:1147-1158(2013) C18 ORF1, a novel negative regulator of transforming growth factor-beta signaling.Nakano N., Maeyama K., Sakata N., Itoh F., Akatsu R., Nakata M., Katsu Y., Ikeno S., Togawa Y., Vo Nguyen T.T., Watanabe Y., Kato M., Itoh S.J. Biol. Chem. 289:12680-12692(2014) TGF-beta signal transduction.Massague J.Annu. Rev. Biochem. 67:753-791(1998) Remarkable versatility of Smad proteins in the nucleus of transforming growth factor-beta activated cells.Verschueren K., Huylebroeck D.Cytokine Growth Factor Rev. 10:187-199(1999) The Smad pathway.Wrana J.L., Attisano L.Cytokine Growth Factor Rev. 11:5-13(2000) TGF-beta signaling by Smad proteins.Miyazono K.Cytokine Growth Factor Rev. 11:15-22(2000) Structural basis of Smad2 recognition by the Smad anchor for receptor activation.Wu G., Chen Y.-G., Ozdamar B., Gyuricza C.A., Chong P.A., Wrana J.L., Massague J., Shi Y.Science 287:92-97(2000) Structural basis of heteromeric smad protein assembly in TGF-beta signaling.Chacko B.M., Qin B.Y., Tiwari A., Shi G., Lam S., Hayward L.J., De Caestecker M., Lin K.Mol. Cell 15:813-823(2004) The consensus coding sequences of human breast and colorectal cancers.Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.Science 314:268-274(2006) +Additional computationally mapped references.<p>Provides general information on the entry.

Other Notes

Small volumes of SMAD2 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for SMAD2 purchase

MBS719384 is a recombinant protein targeting SMAD2. Also known as Recombinant Human Mothers against decapentaplegic homolog 2 protein. Host: E Coli.

Additional Details

NCBI/Uniprot data below describe general gene information for SMAD2. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Related Accession #
GenBank Nucleotide #
NCBI Official Full Name
mothers against decapentaplegic homolog 2 isoform 1
NCBI Official Synonym Full Names
SMAD family member 2
NCBI Official Symbol
SMAD2
NCBI Official Synonym Symbols
JV18; MADH2; MADR2; JV18-1; hMAD-2; hSMAD2
UniProt Protein Name
Mothers against decapentaplegic homolog 2
UniProt Synonym Protein Names
JV18-1; Mad-related protein 2; hMAD-2; SMAD family member 2; SMAD 2; Smad2; hSMAD2
UniProt Gene Name
SMAD2
UniProt Synonym Gene Names
MADH2; MADR2; MAD homolog 2; Mothers against DPP homolog 2; hMAD-2; SMAD 2; Smad2; hSMAD2
UniProt Entry Name
SMAD2_HUMAN
NCBI Protein Information
mothers against decapentaplegic homolog 2

NCBI Summary for SMAD2

The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signal of the transforming growth factor (TGF)-beta, and thus regulates multiple cellular processes, such as cell proliferation, apoptosis, and differentiation. This protein is recruited to the TGF-beta receptors through its interaction with the SMAD anchor for receptor activation (SARA) protein. In response to TGF-beta signal, this protein is phosphorylated by the TGF-beta receptors. The phosphorylation induces the dissociation of this protein with SARA and the association with the family member SMAD4. The association with SMAD4 is important for the translocation of this protein into the nucleus, where it binds to target promoters and forms a transcription repressor complex with other cofactors. This protein can also be phosphorylated by activin type 1 receptor kinase, and mediates the signal from the activin. Alternatively spliced transcript variants have been observed for this gene. [provided by RefSeq, May 2012]
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UniProt Comments for SMAD2

SMAD2: ubiquitously expressed transcription factor phosphorylated and activated by TGF-beta receptor-type kinases. Participates in a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation and apoptosis. Phosphorylated Smads dimerize with collaborating Smad4 and are translocated into the nucleus, where the transcription of target genes is stimulated. Two alternatively spliced isoforms have been described.

Protein type: DNA-binding; Transcription factor

Chromosomal Location of Human Ortholog: 18q21.1

Cellular Component: cytoplasm; cytosol; nuclear chromatin; nucleoplasm; nucleus; transcription factor complex

Molecular Function: chromatin binding; DNA binding; double-stranded DNA binding; metal ion binding; phosphatase binding; protein binding; protein heterodimerization activity; protein homodimerization activity; SMAD binding; transcription activator binding; transcription factor activity; transcription factor binding; transforming growth factor beta receptor binding; transforming growth factor beta receptor, pathway-specific cytoplasmic mediator activity; ubiquitin protein ligase binding

Biological Process: activin receptor signaling pathway; anterior/posterior pattern formation; cell fate commitment; common-partner SMAD protein phosphorylation; embryonic cranial skeleton morphogenesis; embryonic foregut morphogenesis; endoderm formation; gastrulation; gene expression; in utero embryonic development; insulin secretion; lung development; mesoderm formation; negative regulation of cell proliferation; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; negative regulation of transforming growth factor beta receptor signaling pathway; organ growth; palate development; pancreas development; paraxial mesoderm morphogenesis; pericardium development; positive regulation of BMP signaling pathway; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-dependent; post-embryonic development; primary microRNA processing; regulation of binding; regulation of transforming growth factor beta receptor signaling pathway; response to glucose stimulus; SMAD protein complex assembly; somatic stem cell maintenance; transcription initiation from RNA polymerase II promoter; transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway; ureteric bud development; zygotic determination of dorsal/ventral axis
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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