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AB85329

Recombinant Human Smad2 protein

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(1 Publication)

Recombinant Human Smad2 protein is a Human Full Length protein, in the 1 to 467 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.

View Alternative Names

MADH2, MADR2, SMAD2, Mothers against decapentaplegic homolog 2, MAD homolog 2, Mothers against DPP homolog 2, JV18-1, Mad-related protein 2, SMAD family member 2, hMAD-2, SMAD 2, Smad2, hSMAD2

1 Images
SDS-PAGE - Recombinant Human Smad2 protein (AB85329)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Smad2 protein (AB85329)

15% SDS-PAGE analysis of 3μg ab85329

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q15796

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.58% Sodium chloride, 0.316% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTPNTIDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS","proteinLength":"Full Length","predictedMolecularWeight":"54.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":467,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"Q15796","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Smad2 also known as Mothers against decapentaplegic homolog 2 (MAD2) or MADR2 is a signaling protein involved in the transforming growth factor-beta (TGF-β) receptor pathway. Smad2 has a molecular mass of approximately 58 kDa and expresses in various tissues including epithelial mesenchymal and endothelial cells. Smad2 undergoes phosphorylation on serine residues in response to TGF-β signaling converting it into phosphorylated forms often referred to as p-Smad2 or phospho-Smad2. These phosphorylated forms are critical for the relay of signals from the cell surface to the nucleus.
Biological function summary

Smad2 acts as an intracellular mediator for TGF-β signaling a pathway important for regulating cell proliferation differentiation and apoptosis. Smad2 typically functions as part of a heteromeric complex with Smad4 another key player in TGF-β signaling. Upon activation phosphorylated Smad2 combines with Smad4 to form a complex that translocates into the nucleus. This complex then binds to specific DNA sequences to regulate the transcription of target genes involved in processes such as cell growth inhibition and extracellular matrix production.

Pathways

Smad2 is integral to the TGF-β and activin receptor signaling pathways. These pathways are essential in controlling cell growth and immune responses. Smad2 interacts with other proteins such as Smad3 in addition to Smad4 to modulate gene expression effectively. The interaction between Smad2 and these proteins ensures precise control of cellular responses to external stimuli emphasizing its pivotal role in maintaining cellular homeostasis.

Smad2 correlates with various pathological conditions including fibrosis and cancer. Aberrant Smad2 signaling can contribute to the development of these diseases as excessive TGF-β signaling promotes fibrotic tissue deposition and tumor progression. Smad2 connects with other proteins like Smad3 in these pathological contexts both acting as mediators of abnormal cellular behaviors. Understanding the regulatory mechanisms of Smad2 can help develop therapeutic strategies against disorders linked to dysregulated TGF-β signaling.

Specifications

Form

Liquid

Additional notes

ab85329 was purified using conventional chromatography techniques.

General info

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 SMAD2/SMAD4 complex, activates transcription. Promotes TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells (By similarity). Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. May act as a tumor suppressor in colorectal carcinoma (PubMed : 8752209).

Sequence similarities

Belongs to the dwarfin/SMAD family.

Post-translational modifications

Phosphorylated on one or several of Thr-220, Ser-245, Ser-250, and Ser-255. In response to TGF-beta, phosphorylated on Ser-465/467 by TGF-beta and activin type 1 receptor kinases. TGF-beta-induced Ser-465/467 phosphorylation declines progressively in a KMT5A-dependent manner. Able to interact with SMURF2 when phosphorylated on Ser-465/467, recruiting other proteins, such as SNON, for degradation. In response to decorin, the naturally occurring inhibitor of TGF-beta signaling, phosphorylated on Ser-240 by CaMK2. Phosphorylated by MAPK3 upon EGF stimulation; which increases transcriptional activity and stability, and is blocked by calmodulin. Phosphorylated by PDPK1.. In response to TGF-beta, ubiquitinated by NEDD4L; which promotes its degradation. Monoubiquitinated, leading to prevent DNA-binding (By similarity). Deubiquitination by USP15 alleviates inhibition and promotes activation of TGF-beta target genes (PubMed:21947082). Ubiquitinated by RNF111, leading to its degradation: only SMAD2 proteins that are 'in use' are targeted by RNF111, RNF111 playing a key role in activating SMAD2 and regulating its turnover (By similarity).. Acetylated on Lys-19 by coactivators in response to TGF-beta signaling, which increases transcriptional activity. Isoform short: Acetylation increases DNA binding activity in vitro and enhances its association with target promoters in vivo. Acetylation in the nucleus by EP300 is enhanced by TGF-beta.

Subcellular localisation

Nucleus

Product protocols

Target data

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 SMAD2/SMAD4 complex, activates transcription. Promotes TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells (By similarity). Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. May act as a tumor suppressor in colorectal carcinoma (PubMed : 8752209).
See full target information SMAD2

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Nature genetics 56:420-430 PubMed38378865

2024

Functional dissection of human cardiac enhancers and noncoding de novo variants in congenital heart disease.

Applications

Unspecified application

Species

Unspecified reactive species

Feng Xiao,Xiaoran Zhang,Sarah U Morton,Seong Won Kim,Youfei Fan,Joshua M Gorham,Huan Zhang,Paul J Berkson,Neil Mazumdar,Yangpo Cao,Jian Chen,Jacob Hagen,Xujie Liu,Pingzhu Zhou,Felix Richter,Yufeng Shen,Tarsha Ward,Bruce D Gelb,Jonathan G Seidman,Christine E Seidman,William T Pu
View all publications

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