Rhesus Recombinant CD160 protein, His Tag (V2LY-0526-LY9664)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Rhesus
Tag
His Tag
Protein Construction
This product is Rhesus Recombinant CD160 protein, His Tag consist of Amino Acid: 1-158 and predicts a molecular mass of 16.3 kDa.
Molecule Mass
16.3 kDa
Sequence
Amino Acid: 1-158
Species
Rhesus

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>90% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Tris, NaCl, Glutathione, EDTA, DTT, PMSF, Glycerol
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
CD160 Molecule
Function
Receptor on immune cells capable to deliver stimulatory or inhibitory signals that regulate cell activation and differentiation. Exists as a GPI-anchored and as a transmembrane form, each likely initiating distinct signaling pathways via phosphoinositol 3-kinase in activated NK cells and via LCK and CD247/CD3 zeta chain in activated T cells (PubMed:19109136, PubMed:11978774, PubMed:17307798).
Receptor for both classical and non-classical MHC class I molecules (PubMed:9973372, PubMed:12486241).
In the context of acute viral infection, recognizes HLA-C and triggers NK cell cytotoxic activity, likely playing a role in anti-viral innate immune response (PubMed:12486241).
On CD8+ T cells, binds HLA-A2-B2M in complex with a viral peptide and provides a costimulatory signal to activated/memory T cells (PubMed:9973372).
Upon persistent antigen stimulation, such as occurs during chronic viral infection, may progressively inhibit TCR signaling in memory CD8+ T cells, contributing to T cell exhaustion (PubMed:25255144).
On endothelial cells, recognizes HLA-G and controls angiogenesis in immune privileged sites (PubMed:16809620).
Receptor or ligand for TNF superfamily member TNFRSF14, participating in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. Upon ligation of TNFRSF14, provides stimulatory signal to NK cells enhancing IFNG production and anti-tumor immune response (By similarity).
On activated CD4+ T cells, interacts with TNFRSF14 and downregulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (PubMed:18193050).
In the context of bacterial infection, acts as a ligand for TNFRSF14 on epithelial cells, triggering the production of antimicrobial proteins and proinflammatory cytokines (By similarity).
Biological Process
Adaptive immune response Source: UniProtKB-KW
Angiogenesis Source: UniProtKB-KW
Defense response to Gram-negative bacterium Source: Ensembl
Innate immune response Source: UniProtKB-KW
Mucosal immune response Source: Ensembl
Negative regulation of adaptive immune memory response Source: UniProtKB
Negative regulation of angiogenesis Source: UniProtKB
Negative regulation of CD4-positive, alpha-beta T cell costimulation Source: UniProtKB
Negative regulation of T cell receptor signaling pathway Source: UniProtKB
Phosphatidylinositol 3-kinase signaling Source: UniProtKB
Positive regulation of endothelial cell apoptotic process Source: UniProtKB
Positive regulation of interferon-gamma production Source: Ensembl
Positive regulation of natural killer cell cytokine production Source: UniProtKB
Positive regulation of natural killer cell degranulation Source: UniProtKB
Positive regulation of natural killer cell mediated cytotoxicity Source: UniProtKB
Positive regulation of natural killer cell mediated immune response to tumor cell Source: Ensembl
Regulation of immune response Source: Reactome
T cell costimulation Source: UniProtKB
Cellular Location
Cell membrane; Secreted. Released from the cell membrane by GPI cleavage.

Del Rio, M. L., Nguyen, T. H., Tesson, L., Heslan, J. M., Gutierrez-Adan, A., Fernandez-Gonzalez, R., ... & Rodriguez-Barbosa, J. I. (2021). The impact of CD160 deficiency on alloreactive CD8 T cell responses and allograft rejection. Translational Research.

Lenhartová, S., Nemčovič, M., Šebová, R., Benko, M., Zajonc, D. M., & Nemčovičová, I. (2021). Molecular Characterization of the Native (Non-Linked) CD160–HVEM Protein Complex Revealed by Initial Crystallographic Analysis. Crystals, 11(7), 820.

Piotrowska, M., Spodzieja, M., Kuncewicz, K., Rodziewicz-Motowidło, S., & Orlikowska, M. (2021). CD160 protein as a new therapeutic target in a battle against autoimmune, infectious and lifestyle diseases. Analysis of the structure, interactions and functions. European Journal of Medicinal Chemistry, 113694.

Di Censo, C., Marotel, M., Mattiola, I., Müller, L., Scarno, G., Pietropaolo, G., ... & Sciumè, G. (2021). Granzyme A and CD160 expression delineates ILC1 with graded functions in the mouse liver. European Journal of Immunology, 51(11), 2568-2575.

Anestakis, D., Petanidis, S., Domvri, K., Tsavlis, D., Zarogoulidis, P., & Katopodi, T. (2020). Carboplatin chemoresistance is associated with CD11b+/Ly6C+ myeloid release and upregulation of TIGIT and LAG3/CD160 exhausted T cells. Molecular immunology, 118, 99-109.

Liu, S., Zhang, W., Liu, K., & Wang, Y. (2020). CD160 expression on CD8+ T cells is associated with active effector responses but limited activation potential in pancreatic cancer. Cancer Immunology, Immunotherapy, 1-9.

Rodriguez-Barbosa, J. I., Schneider, P., Weigert, A., Lee, K. M., Kim, T. J., Perez-Simon, J. A., & Del Rio, M. L. (2019). HVEM, a cosignaling molecular switch, and its interactions with BTLA, CD160 and LIGHT. Cellular & molecular immunology, 16(7), 679-682.

Liu, W., Garrett, S. C., Fedorov, E. V., Ramagopal, U. A., Garforth, S. J., Bonanno, J. B., & Almo, S. C. (2019). Structural basis of CD160: HVEM recognition. Structure, 27(8), 1286-1295.

Kuncewicz, K., Spodzieja, M., Sieradzan, A., Karczyńska, A., Dąbrowska, K., Dadlez, M., ... & Rodziewicz-Motowidło, S. (2019). A structural model of the immune checkpoint CD160–HVEM complex derived from HDX-mass spectrometry and molecular modeling. Oncotarget, 10(4), 536.

Muscate, F., Stetter, N., Schramm, C., Schulze zur Wiesch, J., Bosurgi, L., & Jacobs, T. (2018). HVEM and CD160: regulators of immunopathology during malaria blood-stage. Frontiers in immunology, 9, 2611.

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For research use only. Not intended for any clinical use.

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