Recombinant Proteins
Product List
SH2D1A Human
SH2 domain containing 1A Human Recombinant
SH2D1B Human
SH2 domain containing 1B Human Recombinant
SH2D1B Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 141 amino acids (1-132a.a.) and having a molecular mass of 16.4kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SH2D1B is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Introduction
The Src Homology 2 (SH2) domain is a structurally conserved protein domain found in many intracellular signal-transducing proteins. It typically consists of approximately 100 amino acids and is characterized by a central antiparallel β-sheet flanked by two α-helices . SH2 domains are primarily known for their ability to bind to phosphorylated tyrosine residues on other proteins, thereby modifying the function or activity of the SH2-containing protein . These domains are especially common in adaptor proteins that aid in the signal transduction of receptor tyrosine kinase pathways .
Key Biological Properties: SH2 domains are pivotal in cell signaling due to their ability to recognize and bind phosphorylated tyrosine residues . This post-translational modification is a key regulator of numerous physiological and molecular pathways in eukaryotic cells .
Expression Patterns and Tissue Distribution: SH2 domains are found in over 100 human proteins and are conserved across a wide range of organisms . They are not present in yeast and appear at the boundary between protozoa and animalia . A detailed bioinformatic examination reveals 120 SH2 domains contained within 115 proteins encoded by the human genome .
Primary Biological Functions: SH2 domains play a crucial role in signal transduction by binding to phosphorylated tyrosine residues, thereby facilitating protein-protein interactions that govern various cellular functions .
Role in Immune Responses and Pathogen Recognition: SH2 domains are involved in immune responses by mediating the signaling pathways of receptor tyrosine kinases, which are essential for the activation and regulation of immune cells .
Mechanisms with Other Molecules and Cells: SH2 domains bind to phosphotyrosine-containing peptides through a strictly conserved Arg residue that pairs with the negatively charged phosphate on the phosphotyrosine . This interaction is central to the propagation of signaling by receptor and non-receptor tyrosine kinases .
Binding Partners and Downstream Signaling Cascades: The binding of an SH2 domain to its cognate tyrosine-phosphorylated target links receptor activation to downstream signaling, both to the nucleus to regulate gene expression and throughout the cytoplasm of the cell .
Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of SH2 domains are regulated by various mechanisms, including transcriptional regulation and post-translational modifications . Tyrosine phosphorylation, a key post-translational modification, is primarily mediated by protein tyrosine kinases (PTKs) and is crucial for the regulation of numerous molecular and physiological pathways .
Biomedical Research: SH2 domains are extensively used in protein engineering to create protein assemblies and study protein-protein interactions .
Diagnostic Tools and Therapeutic Strategies: SH2 domains have applications in diagnostics and therapeutics due to their role in signal transduction pathways. They are used in affinity-purification coupled to mass spectrometry (AP-MS) experiments, microscopy, and synthetic biology .
Role Throughout the Life Cycle: SH2 domains play a significant role throughout the life cycle, from development to aging and disease. They are involved in various cellular processes such as cell proliferation, differentiation, and response to external stimuli . Dysregulation of SH2 domain-mediated interactions can lead to several pathologies, highlighting their importance in maintaining cellular homeostasis .
