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ELISA Kit for Rat Mothers against decapentaplegic homolog 3

SKU : BHE13809795

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E2185r
Alternative Names	SMAD family member 3 ; SMAD 3 ; Madh3
Categories	Elisa
Function	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 are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures.
Specificity	Natural and recombinant Rat Mothers against decapentaplegic homolog 3
Subcellular Location	Cytoplasm Nucleus Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. Through the action of the phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out of the nucleus by interaction with RANBP1. Co-localizes with LEMD3 at the nucleus inner membrane. MAPK-mediated phosphorylation appears to have no effect on nuclear import.
Detection Range	0.312-20ng/mL
Entryname	SMAD3_RAT
Method Type	Sandwich
Platform	PF03165
Protein Name	Mothers against decapentaplegic homolog 3
Sensitivity	0.196ng/mL
Sequence	50: MSSILPFTPP ; IVKRLLGWKK ; GEQNGQEEKW ; CEKAVKSLVK ; KLKKTGQLDE ; 100: LEKAITTQNV ; NTKCITIPRS ; LDGRLQVSHR ; KGLPHVIYCR ; LWRWPDLHSH ; 150: HELRAMELCE ; FAFNMKKDEV ; CVNPYHYQRV ; ETPVLPPVLV ; PRHTEIPAEF ; 200: PPLDDYSHSI ; PENTNFPAGI ; EPQSNIPETP ; PPGYLSEDGE ; TSDHQMNHSM ; 250: DAGSPNLSPN ; PMSPAHNNLD ; LQPVTYCEPA ; FWCSISYYEL ; NQRVGETFHA ; 300: SQPSMTVDGF ; TDPSNSERFC ; LGLLSNVNRN ; AAVELTRRHI ; GRGVRLYYIG ; 350: GEVFAECLSD ; SAIFVQSPNC ; NQRYGWHPAT ; VCKIPPGCNL ; KIFNNQEFAA ; 400: LLAQSVNQGF ; EAVYQLTRMC ; TIRMSFVKGW ; GAEYRRQTVT ; STPCWIELHL ; 425: NGPLQWLDKV ; LTQMGSPSIR ; CSSVS
Sequence Length	425
String	P84025
Sub Unit	Monomer; in the absence of TGF-beta (By similarity). Homooligomer; in the presence of TGF-beta (By similarity). Heterotrimer; forms a heterotrimer in the presence of TGF-beta consisting of two molecules of C-terminally phosphorylated SMAD2 or SMAD3 and one of SMAD4 to form the transcriptionally active SMAD2/SMAD3-SMAD4 complex (By similarity). Interacts with TGFBR1 (By similarity). Interacts (via the MH2 domain) with ZFYVE9. Interacts with HDAC1, VDR, TGIF and TGIF2, RUNX3, CREBBP, SKOR1, SKOR2, SNON, ATF2 and SMURF2. Interacts with DACH1; the interaction inhibits the TGF-beta signaling. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3. Forms a complex with SMAD2 and TRIM33 upon addition of TGF-beta. Found in a complex with SMAD3, RAN and XPO4. Interacts in the complex directly with XPO4. Interacts (via the MH2 domain) with LEMD3; the interaction represses SMAD3 transcriptional activity through preventing the formation of the heteromeric complex with SMAD4 and translocation to the nucleus. Interacts with RBPMS. Interacts (via MH2 domain) with MECOM. Interacts with WWTR1 (via its coiled-coil domain). Interacts (via the linker region) with EP300 (C-terminal); the interaction promotes SMAD3 acetylation and is enhanced by TGF-beta phosphorylation in the C-terminal of SMAD3. This interaction can be blocked by competitive binding of adenovirus oncoprotein E1A to the same C-terminal site on EP300, which then results in partially inhibited SMAD3/SMAD4 transcriptional activity. Interacts with SKI; the interaction represses SMAD3 transcriptional activity. Component of the multimeric complex SMAD3/SMAD4/JUN/FOS which forms at the AP1 promoter site; required for syngernistic transcriptional activity in response to TGF-beta. Interacts (via an N-terminal domain) with JUN (via its basic DNA binding and leucine zipper domains); this interaction is essential for DNA binding and cooperative transcriptional activity in response to TGF-beta. Interacts with PPM1A; the interaction dephosphorylates SMAD3 in the C-terminal SXS motif leading to disruption of the SMAD2/3-SMAD4 complex, nuclear export and termination of TGF-beta signaling. Interacts (dephosphorylated form via the MH1 and MH2 domains) with RANBP3 (via its C-terminal R domain); the interaction results in the export of dephosphorylated SMAD3 out of the nucleus and termination of the TGF-beta signaling. Interacts with AIP1, PML, TGFB1I1, TTRAP, FOXL2, PRDM16, HGS and WWP1. Interacts with NEDD4L; the interaction requires TGF-beta stimulation (By similarity). Interacts with MEN1. Interacts (via MH2 domain) with CITED2 (via C-terminus).

Uniprot	P84025
Gene Name	Smad3
Immunogen Species	Rattus norvegicus (Rat)
Kegg	rno:25631
Unigene	Rn.10636

Reference	1. "Regulation of transforming growth factor beta- and activin-induced transcription by mammalian Mad proteins." Chen Y., Lebrun J.-J., Vale W.W. Proc. Natl. Acad. Sci. U.S.A.93:12992-12997(1996) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];FUNCTION;SUBCELLULAR LOCATION tissue: Brain. 2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res.14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] tissue: Prostate. 3. "Inactivation of menin, a Smad3-interacting protein, blocks transforming growth factor type beta signaling." Kaji H., Canaff L., Lebrun J.J., Goltzman D., Hendy G.N. Proc. Natl. Acad. Sci. U.S.A.98:3837-3842(2001) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH MEN1 4. "Cited2 modulates TGF-beta-mediated upregulation of MMP9." Chou Y.T., Wang H., Chen Y., Danielpour D., Yang Y.C. Oncogene25:5547-5560(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH CITED2

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