Recombinant Proteins
Product List
ULBP1 Human
UL16 Binding Protein 1 Human Recombinant
ULBP1 Human, Sf9
UL16 Binding Protein 1 Human Recombinant, Sf9
ULBP1 is fused to a 6 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
ULBP2 Human
UL16 Binding Protein 2 Human Recombinant
ULBP2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
ULBP2 Human, Sf9
UL16 Binding Protein 2 Human Recombinant, Sf9
ULBP3 Human
UL16 Binding Protein 3 Human Recombinant
ULBP3 Human, Sf9
UL16 Binding Protein 3 Human Recombinant, Sf9
ULBP3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 430 amino acids (30-217a.a) and having a molecular mass of 49.3kDa.
ULBP3 is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Sterile filtered colorless solution.
ULBP4 Human
UL16 Binding Protein 4 Human Recombinant
Introduction
UL16 binding proteins (ULBPs) are a family of MHC class I-related molecules that were initially identified as targets of the human cytomegalovirus (HCMV) glycoprotein, UL16 . These proteins are also known as retinoic acid early transcripts (RAET1) and are ligands for the NKG2D receptor, an activating receptor expressed on natural killer (NK) cells and certain T cells . The ULBP family includes several members, such as ULBP1, ULBP2, and ULBP3, each with distinct but related functions .
Key Biological Properties: ULBPs are glycoproteins that are structurally related to MHC class I molecules but lack the α3 domain and the transmembrane segment . They are anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) anchor .
Expression Patterns and Tissue Distribution: ULBPs are expressed on the surface of various cell types, including tumor cells and cells under stress conditions such as infection . They are frequently upregulated in response to cellular stress, infection, and transformation . For example, ULBP1 is upregulated during HCMV infection .
Primary Biological Functions: ULBPs function as stress-induced ligands for the NKG2D receptor, mediating the activation of NK cells and certain T cells . This interaction plays a crucial role in immune surveillance by enabling the immune system to recognize and eliminate stressed, infected, or transformed cells .
Role in Immune Responses and Pathogen Recognition: By binding to the NKG2D receptor, ULBPs activate NK cells and cytotoxic T cells, leading to the destruction of target cells . This mechanism is vital for the immune response against tumors and viral infections .
Mechanisms with Other Molecules and Cells: ULBPs interact with the NKG2D receptor on NK cells and certain T cells . This binding triggers a series of downstream signaling cascades that result in the activation of these immune cells .
Binding Partners and Downstream Signaling Cascades: Upon binding to NKG2D, ULBPs induce marked protein tyrosine phosphorylation and activate several signaling pathways, including the Janus kinase 2 (JAK2), STAT5, extracellular signal-regulated kinase (ERK), mitogen-activated protein kinase (MAPK), and phosphatidylinositol 3-kinase (PI3K)/Akt pathways . These pathways are crucial for the activation and function of NK cells and cytotoxic T cells .
Regulatory Mechanisms Controlling Expression and Activity: The expression of ULBPs is regulated at both the transcriptional and post-transcriptional levels . For instance, the unfolded protein response pathways during endoplasmic reticulum (ER) stress can upregulate ULBP expression via the protein kinase RNA-like ER kinase-activating factor 4-C/EBP homologous protein (PERK-ATF4-CHOP) pathway .
Transcriptional Regulation and Post-Translational Modifications: ULBPs undergo various post-translational modifications, including glycosylation, which are essential for their stability and function . Additionally, the proteolytic release of soluble ULBPs from tumor cells can modulate their activity and availability .
Biomedical Research: ULBPs are valuable tools in studying immune responses and the mechanisms of immune surveillance . They are frequently used in research to understand how the immune system recognizes and eliminates stressed or transformed cells .
Diagnostic Tools and Therapeutic Strategies: ULBPs have potential applications in cancer immunotherapy and the development of diagnostic tools for detecting tumors and infections . Their ability to activate NK cells and cytotoxic T cells makes them promising candidates for therapeutic interventions .
Role Throughout the Life Cycle: ULBPs play a critical role in immune surveillance throughout the life cycle, from development to aging and disease . Their expression and activity are tightly regulated to ensure the effective elimination of stressed, infected, or transformed cells while avoiding damage to normal tissues .
