|Detection of Human PILR‑ alpha by Western Blot. Western blot shows lysates of human peripheral blood mononuclear cells (PBMCs), human spleen tissue, human lung tissue, CEM human T-lymphoblastoid cell line, and U937 human histiocytic lymphoma cell line. PVDF membrane was probed with 2 µg/mL of Rabbit Anti-Human PILR‑ alpha Monoclonal Antibody (Catalog # MAB64841) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for PILR‑ alpha at approximately 35-50 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Detection of PILR-alpha R in HEK293 Human Cell Line Transfected with Human PILR-alpha and eGFP by Flow Cytometry HEK293 human embryonic kidney cell line transfected with either (A) human PILR-alpha or (B) irrelevant transfectants and eGFP was stained with Rabbit Anti-Human PILR-alpha Monoclonal Antibody (Catalog # MAB64841) followed by Allophycocyanin-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # F0111). Quadrant markers were set based on control antibody staining (Catalog # MAB1050). View our protocol for Staining Intracellular Molecules.|
|PILR‑ alpha in Human Tonsil. PILR‑ alpha was detected in immersion fixed paraffin-embedded sections of human tonsil using Rabbit Anti-Human PILR‑ alpha Monoclonal Antibody (Catalog # MAB64841) at 3 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC003). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to dendritic cells. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.|
Paired immunoglobulin-like type 2 receptor alpha (PILRa; also inhibitory receptor PILR-alpha) are 44-50 kDa paired receptors that consist of highly related activating and inhibitory receptors, and are widely involved in the regulation of the immune system. PILR-alpha is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Human PILR-alpha is synthesized as a 303 amino acid (aa) precursor that contains a 19 aa signal sequence, a 178 aa extracellular domain (ECD), a 21 aa transmembrane segment, and an 85 aa cytoplasmic domain. The ECD contains one Ig-like V-type domain and one potential site for N-linked glycosylation. The cytoplasmic domain contains two ITIM motifs (aa 267-272 and 296-301). Alternate splicing generates multiple shorter isoforms. One is TM and possesses a 35 aa substitution for aa 264-303, while others are soluble, and show a deletion of aa 152-224 that may be coupled to the 35 aa substitution noted above, or simply exhibit a 24 aa substitution for aa 152-303. Mature human PILR-alpha is 45% aa identical to mature mouse PILR-alpha. PILR-alpha is predominantly detected in hemopoietic tissues and is expressed in monocytes, macrophages, and granulocytes, but not lymphocytes. It is also strongly expressed by dendritic cells. PILR-alpha interacts with herpes simplex 1 glycoprotein B and functions as an entry coreceptor for this virus.
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