shp 2

SHP2, also known as PTPN11, belongs to the protein-tyrosine phosphatase(PTP) family, non-receptor class 2 subfamily. PTPs catalyze the removal of phosphate groups from tyrosine residues by the hydrolysis of phosphoric acid monoesters. They dephosphorylate EGFR, JAK2 and TYK2 kinases, promoting oncogenic transformation. SHP2 is widely expressed, with highest levels in heart, brain, and skeletal muscle. SHP2 acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. It also dephosphorylates ROCK2 at Tyr-722 resulting in stimulation of its RhoA binding activity.

B- and T-lymphocyte attenuator (BTLA; CD272) is a 35 kDa type I transmembrane glycoprotein in the CD28 family of T cell costimulatory molecules. BTLA is a inhibitory receptor on lymphocytes that negatively regulates antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2. BTLA may interact in cis (on the same cell) or in trans (on other cells) with TNFRSF14. BTLA Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 16.7 kDa and the accession number is Q7Z6A9-1.

Acts as an inhibitory receptor for myeloid cells and mast cells. Positively regulates the phagocytosis of apoptotic cells (efferocytosis) via phosphatidylserine (PS) recognition; recognizes and binds PS as a ligand which is expressed on the surface of apoptotic cells. Plays an important role in the maintenance of immune homeostasis, by promoting macrophage-mediated efferocytosis and by inhibiting dendritic cell-mediated efferocytosis. Negatively regulates Fc epsilon receptor-dependent mast cell activation and allergic responses via binding to ceramide and sphingomyelin which act as ligands. May act as a coreceptor for interleukin 4 (IL-4). Associates with and regulates IL-4 receptor alpha-mediated responses by augmenting IL-4- and IL-13-induced signaling. Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 and TRIF through activation of PTPN6/SHP-1 and PTPN11/SHP-2. Inhibits osteoclast formation. Induces macrophage cell death upon engagement.

Members of the immunoglobulin-like transcript (ILT) family are activating and inhibitory immunoreceptors whose genes are located same locus that encodes killer cell Ig-like receptors (KIR). Leukocyte Immunoglobulin-Like Receptor Subfamily B Member 2 (LIR-2) is a type I transmembrane protein. LIR-2 is expressed primarily on monocytes and dendritic cells (DC). Human LIR-2 is produced as a 598 amino acino acid precursor including a 21 aa signal sequence, a 440 aa extracellular domain (ECD), a 21 aa transmenbrane segment, and a 116 aa cytoplasmic domain. LIR-2 binds to Classical MHCI proteins. Ligation of LIR-2 incluces Tyr phosphorylation within its cytoplasmic ITIMs, a requirement for association with SHP-1. LIR-2 mediates tolerogenic DC-induced CD4+ T cell energy in vitro and in vivo.

Myelin protein zero-like protein 1(MPZL1) is encoded by the MPZL1 gene, which is a single-pass type I membrane protein. It is widely expressed with highest levels in heart, placenta, kidney and pancreas. As cell surface receptor, it involved in signal transduction processes. MPZL1 recruits PTPN11/SHP-2 to the cell membrane and subsequently activate/phosphorylate Src kinase at Tyr426, promoting phosphorylation of cortactin and migration of HCC cells. MPZL1also is a major receptor for concanavalin-A (ConA) and involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases.

B- and T-lymphocyte attenuator (BTLA; CD272) is a 35 kDa type I transmembrane glycoprotein in the CD28 family of T cell costimulatory molecules. BTLA is a inhibitory receptor on lymphocytes that negatively regulates antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2. BTLA may interact in cis (on the same cell) or in trans (on other cells) with TNFRSF14. BTLA Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 15.04 kDa and the accession number is A0A2K5W7M7.

Signaling lymphocyte activation molecule (SLAM), is a self-ligand glycoprotein which exists not only found on the surface of activated and memory T cells, but also on the surface of activated B cells, dendritic cells, and macrophages. SLAM consists of a extracellular domain (ECD) with two Ig-like domains,transmembrane segment, and cytoplasmic domain with three immunoreceptor tyrosine switch motifs (ITSM). SLAM is thought to play an important role in adhesion between T cells and APCs and has been shown to act as a coreceptor in TCR-dependent responses. SLAM, together with CD46, is one of the two receptors for measles virus. SLAM is a cell surface receptor that, like the B cell receptor, CD40, and CD95, can transmit positive or negative signals. SLAM can associate with the SH2-containing inositol phosphatase (SHIP), the SH2-containing protein tyrosine phosphatase (SHP-2), and the adaptor protein SH2 domain protein 1A. It’s upregulated on activated B cells and CD4+ and CD8+ T cells, but downregulated on Th2 polarized cells. Also, it can Inhibits antigen receptor-mediated production of IFN-gamma, but not IL-2, in CD4-/CD8- T-cells.

SIRPB1A (Signal-regulatory protein beta 1A), also known as SIRP beta 1, belongs to signal-regulatory-protein (SIRP) family, and immunoglobulin superfamily. Signal-regulatory proteins (SIRPs) are cell-surface glycoproteins expressed on myeloid and neural cells that have been shown to recruit SH2 domain-containing protein phosphatase 1 (SHP-1) and SHP-2 and to regulate receptor tyrosine kinase-coupled signaling. SIRP are classified as SIRP alpha molecules, containing 11- to 113-amino acid long, or SIRP beta molecules, with a 5-amino acid long intracytoplasmic domain. SIRP beta 1 is a new DAP12-associated receptor involved in the activation of myeloid cells, which contains a short cytoplasmic domain that lacks sequence motifs capable of recruiting SHP-1 and SHP-2. SIRP beta 1 acts as an activating isoform of SIRP alpha molecules, confirming the co-existence of inhibitory ITIM-bearing molecules, recruiting SHP-1 and SHP-2 protein tyrosine phosphatases, and activating counterparts, whose engagement couples to protein tyrosine kinases via ITAM-bearing molecules.s