Human PD-1 Alexa Fluor® 647-conjugated Antibody Summary
Accession # Q15116
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of PD-1 in HEK293 Human Cell Line Transfected with Human PD-1 and eGFP by Flow Cytometry. HEK293 human embryonic kidney cell line transfected with (A) human PD-1 or (B) irrelevant protein and eGFP was stained with Mouse Anti-Human PD‑1 Alexa Fluor® 647‑conjugated Monoclonal Antibody (Catalog # FAB10861R) or (B) Mouse IgG1 Alexa Fluor 647 Isotype Control (Catalog # IC002R). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Programmed Death-1 (PD-1) is a type I transmembrane protein belonging to the CD28/CTLA-4 family of immunoreceptors that mediate signals for regulating immune responses (1). Members of the CD28/CTLA-4 family have been shown to either promote T cell activation (CD28 and ICOS) or downregulate T cell activation (CTLA-4 and PD-1) (2). PD-1 is expressed on activated T cells, B cells, myeloid cells, and on a subset of thymocytes. In vitro, ligation of PD-1 inhibits TCR-mediated T cell proliferation and production of IL-1, IL-4, IL-10, and IFN-gamma. In addition, PD-1 ligation also inhibits BCR mediated signaling. PD-1 deficient mice have a defect in peripheral tolerance and spontaneously develop autoimmune diseases (2, 3). Two B7 family proteins, PD-L1 (also called B7-H1) and PD-L2 (also known as B7-DC), have been identified as PD-1 ligands. Unlike other B7 family proteins, both PD‑L1 and PD‑L2 are expressed in a wide variety of normal tissues including heart, placenta, and activated spleens (4). The wide expression of PD-L1 and PD-L2 and the inhibitor effects on PD-1 ligation indicate that PD-1 might be involved in the regulation of peripheral tolerance and may help prevent autoimmune diseases (2). The human PD-1 gene encodes a 288 amino acid (aa) protein with a putative 20 aa signal peptide, a 148 aa extracellular region with one immunoglobulin-like V‑type domain, a 24 aa transmembrane domain, and a 95 aa cytoplasmic region. The cytoplasmic tail contains two tyrosine residues that form the Immunoreceptor Tyrosine-based Inhibitory Motif (ITIM) and Immunoreceptor Tyrosine-based Switch Motif (ITSM) that are important in mediating PD-1 signaling. Mouse and human PD-1 share approximately 60% aa sequence identity (4).
- Ishida, Y. et al. (1992) EMBO J. 11:3887.
- Nishimura, H. and T. Honjo (2001) Trends in Immunol. 22:265.
- Latchman, Y. et al. (2001) Nature Immun. 2:261.
- Carreno, B.M. and M. Collins (2002) Annu. Rev. Immunol. 20:29.
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