ptpn6

Protein-Tyrosine Phosphatase 1C (PTP1C) belongs to the protein-tyrosine phosphatase family.which is known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP1C is highly expressed in leukocyte cell type. It contains two SH2 domains and one tyrosine-protein phosphatase domain. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. In addition, PTP1C also modulates signaling by tyrosine phosphorylated cell surface receptors.

Interleukin-4 receptor subunit alpha(IL-4RA), alos known as Soluble IL-4 receptor subunit alpha, belongs to the type I cytokine receptor family and type 4 subfamily. It expressed in both Th1 and Th2 cells. It functions as receptor for both interleukin 4 and interleukin 13 and couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and chemokine and mucus production at sites of allergic inflammation. In certain cell types, IL-4RA can signal through activation of insulin receptor substrates, IRS1/IRS2. The functional IL4 receptor is formed by initial binding of IL4 to IL4R. Subsequently it recruits to the complex of the common gamma chain. In immune cells, IL-4RA creates a type I receptor. In non-immune cells, it forms a type II receptor with of IL13RA1. IL4R can also interact with the IL13/IL13RA1 complex to form a similar type II receptor and interacts with the SH2-containing phosphatases, PTPN6/SHIP1, PTPN11/SHIP2 and INPP5D/SHIP.

LAIR1 (leukocyte-associated Ig-like receptor-1, designated CD305) is an approximately 40 kDa type I transmembrane inhibitory glycoprotein belonging to the Ig superfamily.LAIR1 functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation.

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.

Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation.

Triggering Receptor Expressed on Myeloid Cells-Like Protein 1 (TREML1) is a single-pass type I membrane protein. TREML1 precursor contains a 15 amino acid signal peptide, a 147 amino acid extracellular domain with an Ig-like V-type (immunoglobulin-like) domain, and 128 amino acid cytoplasmic domain. It can be expressed exclusively in platelets and megakaryocytes (MKs). It is a cell surface receptor that may play a role in the innate and adaptive immune response. TREML1 Sequestered in cytoplasmic vesicles in resting platelets. TREML1 be transported to the cell surface after stimulation by thrombin. Soluble fragments can be released into the serum by proteolysis. The phosphorylated TREML1 can interact with PTPN6 and PTPN11. TREML1 may participate in maintaining vascular hemostasis and regulating coagulation and inflammation at sites of injury.

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.

Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation

B-Cell Differentiation Antigen CD72 (CD72) is a single-pass type II membrane protein. CD72 exists as a disulfide-linked homodimer and contains one C-type lectin domain. CD72 is expressed on B lineage cells, NK cells, monocytes, dendritic cells, and mast cells. CD72 is a ligand for CD5. CD72 associates with CD5, interacts with PTPN6/SHP-1 and plays a role in B-cell proliferation and differentiation. CD72 associates with CD79A in the B cell antigen receptor (BCR) complex following antigen stimulation and dampens BCR signaling through interactions with the phosphatase SHP-1.

SIRPα is a type I transmembrane glycoprotein.It contains two Ig-like C1-type domains and one Ig-like V-type domain. Mouse SIRP alpha ECD shares 61%, 75%, 62%, 61%, and 59% aa sequence identity with human, rat, equine, bovine, and porcine SIRP alpha, respectively.SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation.

PTPN6 is an enzyme that belongs to the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of PTPN6 contains two tandem Src homolog (SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of PTPN6 with its substrates. PTPN6 is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. It has been shown that PTPN6 interacts with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling.