Smad nuclear-interacting protein 1, FHA domain-containing protein SNIP1, SNIP1, FLJ12553, dJ423B22.2, RP3-423B22.3.
SNIP1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (258-396 a.a.) and having a molecular mass of 18.8kDa.
The SNIP1 is purified by proprietary chromatographic techniques.
Smad nuclear-interacting protein 1, FHA domain-containing protein SNIP1, SNIP1, FLJ12553, dJ423B22.2, RP3-423B22.3.
MGSSHHHHHH SSGLVPRGSH MRWRLYPFKN DEVLPVMYIH RQSAYLLGRH RRIADIPIDH PSCSKQHAVF QYRLVEYTRA DGTVGRRVKP YIIDLGSGNG TFLNNKRIEP QRYYELKEKD VLKFGFSSRE YVLLHESSDT SEIDRKDDED EEEEEEVSDS.
Smad Nuclear Interacting Protein 1 (SNIP1) is a protein encoded by the SNIP1 gene in humans. This protein plays a crucial role in various cellular processes, including transcription regulation, cell proliferation, and immune response. The recombinant form of this protein is produced using recombinant DNA technology, which allows for the expression of the protein in a host organism, typically bacteria or yeast.
SNIP1 contains a coiled-coil motif and a C-terminal forkhead-associated (FHA) domain . The coiled-coil motif is involved in protein-protein interactions, while the FHA domain is known for its role in recognizing phosphopeptides. These structural features enable SNIP1 to interact with various transcriptional coactivators and inhibitors, thereby modulating gene expression.
SNIP1 functions as a transcriptional coactivator that increases the activity of c-Myc, a well-known oncogene . Additionally, it inhibits the signaling pathways of transforming growth factor-beta (TGF-beta) and nuclear factor kappa-B (NF-kB), both of which are critical in regulating immune responses and inflammation .
SNIP1 plays a significant role in several biological processes:
Cell Proliferation and Cancer Progression: By regulating the stability of cyclin D1 mRNA, SNIP1 influences cell cycle progression and proliferation. This regulation is crucial in cancer biology, as dysregulated cell proliferation is a hallmark of cancer .
Immune Regulation: SNIP1 inhibits NF-kB signaling by competing with RELA for binding to CREBBP/EP300. This inhibition is essential in controlling inflammatory responses and maintaining immune homeostasis .
Cardiac Hypertrophy: Recent studies have shown that SNIP1 has protective effects against pressure overload-induced cardiac hypertrophy, fibrosis, and contractile dysfunction. It achieves this by inhibiting NF-kB signaling, which is activated during pathological cardiac hypertrophy .
The recombinant form of SNIP1 is valuable in research and therapeutic applications. By studying the recombinant protein, researchers can gain a deeper understanding of its structure, function, and interactions. This knowledge can lead to the development of novel therapeutic strategies for diseases associated with SNIP1 dysregulation.