Recombinant Proteins

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SMAD4 Human

Mothers Against Decapentaplegic Homolog 4 Human Recombinant

Recombinant SMAD4 Human, produced in E.Coli, is a single polypeptide chain that lacks glycosylation. It comprises 572 amino acids (specifically, residues 1-552) and exhibits a molecular weight of 62.6 kDa. A 20 amino acid His-Tag is fused to the N-terminus of SMAD4. The purification process involves standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT28950
Source
Escherichia Coli.
Appearance
The solution is sterile, colorless, and has been filtered for sterility.

SMAD2 Human

SMAD Family Member 2 Human Recombinant

Recombinant human SMAD2, produced in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 54.4 kDa. It consists of 487 amino acids (1-467) and includes a 20 amino acid His-Tag fused at the N-terminus. Purification is achieved through standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT28783
Source
Escherichia Coli.
Appearance
A clear and colorless solution, sterile-filtered.

SMAD3 Human

Mothers Against Decapentaplegic Homolog 3 Human Recombinant

Recombinant SMAD3, derived from humans and produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 445 amino acids (residues 1-425). With a molecular weight of 50.2 kDa, this protein is characterized by a 20 amino acid His-Tag fused at its N-terminus. The purification process involves standard chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT28862
Source
Escherichia Coli.
Appearance
The SMAD3 protein solution appears as a clear, colorless liquid, devoid of any particulate matter, and has been sterilized through filtration.
Definition and Classification

SMAD proteins are a family of structurally similar proteins that act as the main signal transducers for receptors of the transforming growth factor beta (TGF-β) superfamily. These proteins are crucial for regulating cell development and growth . The name “SMAD” is derived from the homologies to the Caenorhabditis elegans SMA (small worm phenotype) and MAD (Mothers Against Decapentaplegic) family of genes in Drosophila . SMAD proteins are classified into three sub-types:

  • Receptor-regulated SMADs (R-SMADs): Includes SMAD1, SMAD2, SMAD3, SMAD5, and SMAD8/9 .
  • Common partner SMADs (Co-SMADs): SMAD4 is the only known human Co-SMAD .
  • Inhibitory SMADs (I-SMADs): Includes SMAD6 and SMAD7 .
Biological Properties

SMAD proteins are approximately 400-500 amino acids long and consist of two globular regions at the amino and carboxy termini, connected by a linker region . They are primarily located in the cytoplasm but accumulate in the nucleus following TGF-β signaling . R-SMADs and Co-SMADs are involved in direct signaling from the TGF-β receptor, while I-SMADs suppress the activity of R-SMADs . SMAD proteins are expressed in various tissues and play a critical role in cell development and growth .

Biological Functions

SMAD proteins are essential for regulating cell development, growth, and differentiation . They play a central role in integrating TGF-β and BMP signaling with other essential pathways . SMAD proteins are involved in immune responses and pathogen recognition by regulating the expression of genes involved in these processes . They also play a role in the development of the nervous system and the generation of neurological diseases .

Modes of Action

SMAD proteins function as transcription factors and their activities require carboxyl-terminal phosphorylation by TGF-β receptor kinases . Phosphorylation of R-SMADs causes them to dissociate from SARA (SMAD anchor for receptor activation), exposing a nuclear import sequence and promoting their association with Co-SMADs . The SMAD complex then localizes to the nucleus, where it binds to target genes with the help of other associated proteins . I-SMADs negatively regulate R-SMAD signaling by competing for binding to activated type I receptors and inhibiting R-SMAD phosphorylation .

Regulatory Mechanisms

The expression and activity of SMAD proteins are regulated by various mechanisms, including transcriptional regulation and post-translational modifications . Phosphorylation, ubiquitination, sumoylation, acetylation, and poly (ADP)-ribosylation are some of the post-translational modifications that regulate SMAD activity and stability . I-SMADs inhibit the phosphorylation of R-SMADs and promote the ubiquitination and degradation of receptor complexes, thus inhibiting signaling .

Applications

SMAD proteins have significant applications in biomedical research, diagnostic tools, and therapeutic strategies . They are central to the TGF-β signaling pathway, which plays a dual role in cancer progression as both an inhibitor of tumor cell growth and an inducer of tumor metastasis . SMAD proteins are also involved in nerve regeneration and the development of therapeutic strategies for neurological diseases .

Role in the Life Cycle

SMAD proteins play a crucial role throughout the life cycle, from development to aging and disease . They are involved in the development of the nervous system, neuralization of ectodermal cells, and specification of cell types . SMAD proteins also play a role in the generation of neurological diseases and are considered therapeutic targets for the treatment of these diseases .

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