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Signal transducer CD24 also known as cluster of differentiation 24 or heat stable antigen CD24 (HSA) is a protein that in mouse is encoded by the CD24 gene. CD24 is a cell adhesion molecule. CD24 is a sialoglycoprotein expressed at the surface of most B lymphocytes and differentiating neuroblasts. It is also expressed on neutrophils and neutrophil precursors from the myelocyte stage onwards. The encoded protein is anchored via a glycosyl phosphatidylinositol (GPI) link to the cell surface. The protein also contributes to a wide range of downstream signaling networks and is crucial for neural development. Cross-linking of CD24 on the surface of neutrophils induces apoptosis, and this appears to be defective in sepsis.

Signal transducer CD24 also known as cluster of differentiation 24 or heat stable antigen CD24 (HSA) is a protein that in mouse is encoded by the CD24 gene. CD24 is a cell adhesion molecule. CD24 is a sialoglycoprotein expressed at the surface of most B lymphocytes and differentiating neuroblasts. It is also expressed on neutrophils and neutrophil precursors from the myelocyte stage onwards. The encoded protein is anchored via a glycosyl phosphatidylinositol (GPI) link to the cell surface. The protein also contributes to a wide range of downstream signaling networks and is crucial for neural development. Cross-linking of CD24 on the surface of neutrophils induces apoptosis, and this appears to be defective in sepsis.

Signal transducer CD24 also known as cluster of differentiation 24 or heat stable antigen CD24 (HSA) is a protein that in mouse is encoded by the CD24 gene. CD24 is a cell adhesion molecule. CD24 is a sialoglycoprotein expressed at the surface of most B lymphocytes and differentiating neuroblasts. It is also expressed on neutrophils and neutrophil precursors from the myelocyte stage onwards. The encoded protein is anchored via a glycosyl phosphatidylinositol (GPI) link to the cell surface. The protein also contributes to a wide range of downstream signaling networks and is crucial for neural development. Cross-linking of CD24 on the surface of neutrophils induces apoptosis, and this appears to be defective in sepsis.

The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Rα, IL-2Rβ, and IL-2Rγ. The IL-2Rα is a type I transmembrane protein consisting of a 219 amino acid (a.a.) extracellular domain, a 19 a.a. transmembrane domain and a 13 a.a. intracellular domain, which is not involved in the transduction of IL-2 signal. Activated T cells, regulatory T cells (Tregs) and NK cells express high levels of CD25 and expression of the high-affinity IL-2Rα is mostly limited to these cell populations. Signaling via IL-2Rα mediates multiple biological processes in various cell populations, e.g. proliferation and differentiation of B cells and NK cells. A soluble form of IL-2Rα (IL-2Rα) appears in serum, concomitant with its increased expression on cells. The function of the soluble IL-2Rα is unclear. Increased levels of IL-2Rα in biological fluids reportedly correlate with increased T and B cell activation and immune system activation. Increased serum concentration of IL-2Rα has been observed in patients with a variety of inflammatory conditions and in the course of some leukemias and lymphomas.

The IL-2 receptor system consists of three non-covalently linked subunits termed IL-2Rα, IL-2Rβ, and IL-2Rγ. The IL-2Rα is a type I transmembrane protein consisting of a 219 amino acid (a.a.) extracellular domain, a 19 a.a. transmembrane domain and a 13 a.a. intracellular domain, which is not involved in the transduction of IL-2 signal. Activated T cells, regulatory T cells (Tregs) and NK cells express high levels of CD25 and expression of the high-affinity IL-2Rα is mostly limited to these cell populations. Signaling via IL-2Rα mediates multiple biological processes in various cell populations, e.g. proliferation and differentiation of B cells and NK cells. A soluble form of IL-2Rα (IL-2Rα) appears in serum, concomitant with its increased expression on cells. The function of the soluble IL-2Rα is unclear. Increased levels of IL-2Rα in biological fluids reportedly correlate with increased T and B cell activation and immune system activation. Increased serum concentration of IL-2Rα has been observed in patients with a variety of inflammatory conditions and in the course of some leukemias and lymphomas.

CD70 (Cluster of Differentiation 70) is a protein that in humans is encoded by CD70 gene. CD70 is a ligand for CD27. The CD70-CD27 pathway plays an important role in the generation and maintenance of T cell immunity, in particular during antiviral responses. Upon CD27 binding, induces the proliferation of costimulated T-cells and enhances the generation of cytolytic T-cells.The CD70 protein is expressed on highly activated lymphocytes (like in T- and B-cell lymphomas). It is therefore suggested that anti-CD70 antibodies might be a possible treatment for CD70 positive lymphomas as normal lymphocytes have low CD70 expression.

CD70 (Cluster of Differentiation 70) is a protein that in humans is encoded by CD70 gene. CD70 is a ligand for CD27. The CD70-CD27 pathway plays an important role in the generation and maintenance of T cell immunity, in particular during antiviral responses. Upon CD27 binding, induces the proliferation of costimulated T-cells and enhances the generation of cytolytic T-cells.The CD70 protein is expressed on highly activated lymphocytes (like in T- and B-cell lymphomas). It is therefore suggested that anti-CD70 antibodies might be a possible treatment for CD70 positive lymphomas as normal lymphocytes have low CD70 expression.

Human CD28 is composed of four exons encoding a protein of 220 amino acids that is expressed on the cell surface as a glycosylated, disulfide-linked homodimer of 44 kDa. Members of the CD28 family share a number of common features. These receptors consist of paired V-set immunoglobulin superfamily (IgSF) domains attached to single transmembrane domains and cytoplasmic domains that contain critical signaling motifs. The CD28 and CTLA4 ligands, CD80 and CD86, consist of single V-set and C1-set IgSF domains. The interaction of these costimulatory receptors with ligands is mediated through the MYPPPY motif within the receptor V-set domains. CD28 is expressed constitutively on almost all human CD4 T cells and approximately 50% of CD8 T cells. CD28 costimulation has diverse effects on T cell function, including biochemical events at the immunological synapse, downstream phosphorylation and other post-translational modifications, transcriptional changes, and cytoskeletal remodeling. At the most basic level, CD28 signals increase a cell’s glycolytic rate, allowing cells to generate the energy necessary for growth and proliferation.

Human CD28 is composed of four exons encoding a protein of 220 amino acids that is expressed on the cell surface as a glycosylated, disulfide-linked homodimer of 44 kDa. Members of the CD28 family share a number of common features. These receptors consist of paired V-set immunoglobulin superfamily (IgSF) domains attached to single transmembrane domains and cytoplasmic domains that contain critical signaling motifs. The CD28 and CTLA4 ligands, CD80 and CD86, consist of single V-set and C1-set IgSF domains. The interaction of these costimulatory receptors with ligands is mediated through the MYPPPY motif within the receptor V-set domains. CD28 is expressed constitutively on almost all human CD4 T cells and approximately 50% of CD8 T cells. CD28 costimulation has diverse effects on T cell function, including biochemical events at the immunological synapse, downstream phosphorylation and other post-translational modifications, transcriptional changes, and cytoskeletal remodeling. At the most basic level, CD28 signals increase a cell’s glycolytic rate, allowing cells to generate the energy necessary for growth and proliferation.

CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor family, which regulates proliferation/apoptosis and antibody responses. CD30 is expressed by activated, but not by resting, T and B cells. Aberrant expression of CD30 by mastocytosis mast cells and interaction with its ligand CD30L (CD153) appears to play an important role in the pathogenesis and clinical presentation of systemic mastocytosis. CD30 has been considered as a specific diagnostic biomarker of anaplastic large cell lymphoma (ALCL) and classical Hodgkin lymphoma (cHL). CD30 is also a biomarker used for targeted therapy by an antibody–drug conjugate.

CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor family, which regulates proliferation/apoptosis and antibody responses. CD30 is expressed by activated, but not by resting, T and B cells. Aberrant expression of CD30 by mastocytosis mast cells and interaction with its ligand CD30L (CD153) appears to play an important role in the pathogenesis and clinical presentation of systemic mastocytosis. CD30 has been considered as a specific diagnostic biomarker of anaplastic large cell lymphoma (ALCL) and classical Hodgkin lymphoma (cHL). CD30 is also a biomarker used for targeted therapy by an antibody–drug conjugate.

CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor family, which regulates proliferation/apoptosis and antibody responses. CD30 is expressed by activated, but not by resting, T and B cells. Aberrant expression of CD30 by mastocytosis mast cells and interaction with its ligand CD30L (CD153) appears to play an important role in the pathogenesis and clinical presentation of systemic mastocytosis. CD30 has been considered as a specific diagnostic biomarker of anaplastic large cell lymphoma (ALCL) and classical Hodgkin lymphoma (cHL). CD30 is also a biomarker used for targeted therapy by an antibody–drug conjugate.

CD38 (also referred to as T10 antigen) is a nonlineage-restricted type II transmembrane glycoprotein that has emerged as an intracellular calcium ion mobilizing messenger. It can serve as an ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose. The enzymatic functions of CD38 probably contribute to an array of its immunoregulatory functions. It has been found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B lymphocytes and natural killer cells. Soluble CD38 and the ability of membrane-bound CD38 to become internalized in response to appropriate stimuli suggest that extracellular and intracellular roles for this protein are equally plausible.

CD38 (also referred to as T10 antigen) is a nonlineage-restricted type II transmembrane glycoprotein that has emerged as an intracellular calcium ion mobilizing messenger. It can serve as an ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose. The enzymatic functions of CD38 probably contribute to an array of its immunoregulatory functions. It has been found on the surface of many immune cells (white blood cells), including CD4+, CD8+, B lymphocytes and natural killer cells. Soluble CD38 and the ability of membrane-bound CD38 to become internalized in response to appropriate stimuli suggest that extracellular and intracellular roles for this protein are equally plausible.

CD40 is a costimulatory protein found on antigen presenting cells and is required for their activation. The binding of CD154 (CD40L) on TH cells to CD40 activates antigen presenting cells and induces a variety of downstream effects.CD40 molecule is a potential target for cancer immunotherapy. There are number of completed and ongoing clinical trials where agonistic anti-CD40 monoclonal antibodies are employed to activate an anti-tumor T cell response via activation of dendritic cells.

CD40 Ligand (CD40L/CD154/TRAP) is a membrane glycoprotein and differentiation antigen expressed on the surface of T-cells. The CD40 ligand stimulates B-cell proliferation and secretion of all immunoglobulin isotypes in the presence of cytokines. It also costimulates proliferation of activated T-cell and this is accompanied by the production of IFN-γ, TNF-α, and IL2. CD40 ligand has been shown to induce cytokine production and tumoricidal activity in peripheral blood monocytes.

CD40 Ligand (CD40L/CD154/TRAP) is a membrane glycoprotein and differentiation antigen expressed on the surface of T-cells. The CD40 ligand stimulates B-cell proliferation and secretion of all immunoglobulin isotypes in the presence of cytokines. It also costimulates proliferation of activated T-cell and this is accompanied by the production of IFN-γ, TNF-α, and IL2. CD40 ligand has been shown to induce cytokine production and tumoricidal activity in peripheral blood monocytes.

CD40 Ligand (CD40L/CD154/TRAP) is a membrane glycoprotein and differentiation antigen expressed on the surface of T-cells. The CD40 ligand stimulates B-cell proliferation and secretion of all immunoglobulin isotypes in the presence of cytokines. It also costimulates proliferation of activated T-cell and this is accompanied by the production of IFN-γ, TNF-α, and IL2. CD40 ligand has been shown to induce cytokine production and tumoricidal activity in peripheral blood monocytes.

Leukocyte surface antigen CD47 is also known as Antigenic surface determinant protein OA3, Integrin-associated protein (IAP) and Protein MER6. CD47 contains 1 Ig-like V-type (immunoglobulin-like) domain. CD47 is a 40‑60 kDa variably glycosylated atypical member of the immunoglobulin superfamily and an integral membrane protein that consists of a 123 amino acid (aa) extracellular domain (ECD) with a single Ig-like domain, five membrane-spanning regions with short intervening loops, and a 34 aa C-terminal cytoplasmic tail. CD47 has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins and plays an important role in memory formation and synaptic plasticity in the hippocampus by similarity. CD47 is the receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. CD47 Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation.

Leukocyte surface antigen CD47 is also known as Antigenic surface determinant protein OA3, Integrin-associated protein (IAP) and Protein MER6. CD47 contains 1 Ig-like V-type (immunoglobulin-like) domain. CD47 is a 40‑60 kDa variably glycosylated atypical member of the immunoglobulin superfamily and an integral membrane protein that consists of a 123 amino acid (aa) extracellular domain (ECD) with a single Ig-like domain, five membrane-spanning regions with short intervening loops, and a 34 aa C-terminal cytoplasmic tail. CD47 has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins and plays an important role in memory formation and synaptic plasticity in the hippocampus by similarity. CD47 is the receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. CD47 Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation.

Leukocyte surface antigen CD47 is also known as Antigenic surface determinant protein OA3, Integrin-associated protein (IAP) and Protein MER6. CD47 contains 1 Ig-like V-type (immunoglobulin-like) domain. CD47 is a 40‑60 kDa variably glycosylated atypical member of the immunoglobulin superfamily and an integral membrane protein that consists of a 123 amino acid (aa) extracellular domain (ECD) with a single Ig-like domain, five membrane-spanning regions with short intervening loops, and a 34 aa C-terminal cytoplasmic tail. CD47 has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins and plays an important role in memory formation and synaptic plasticity in the hippocampus by similarity. CD47 is the receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. CD47 Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation.

Leukocyte surface antigen CD47 is also known as Antigenic surface determinant protein OA3, Integrin-associated protein (IAP) and Protein MER6. CD47 contains 1 Ig-like V-type (immunoglobulin-like) domain. CD47 is a 40‑60 kDa variably glycosylated atypical member of the immunoglobulin superfamily and an integral membrane protein that consists of a 123 amino acid (aa) extracellular domain (ECD) with a single Ig-like domain, five membrane-spanning regions with short intervening loops, and a 34 aa C-terminal cytoplasmic tail. CD47 has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins and plays an important role in memory formation and synaptic plasticity in the hippocampus by similarity. CD47 is the receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. CD47 Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation.

CD48 antigen (Cluster of Differentiation 48) also known as B-lymphocyte activation marker (BLAST-1) or signaling lymphocytic activation molecule 2 (SLAMF2) is a protein that in humans is encoded by the CD48 gene. CD48 is a member of the CD2 subfamily of the immunoglobulin superfamily (IgSF) which includes SLAM (signaling lymphocyte activation molecules) proteins, such as CD84, CD150, CD229 and CD244. CD48 is found on the surface of lymphocytes and other immune cells, dendritic cells and endothelial cells, and participates in activation and differentiation pathways in these cells. CD48 was the first B-cell-specific cellular differentiation antigen identified in transformed B lymphoblasts.

CD48 antigen (Cluster of Differentiation 48) also known as B-lymphocyte activation marker (BLAST-1) or signaling lymphocytic activation molecule 2 (SLAMF2) is a protein that in humans is encoded by the CD48 gene. CD48 is a member of the CD2 subfamily of the immunoglobulin superfamily (IgSF) which includes SLAM (signaling lymphocyte activation molecules) proteins, such as CD84, CD150, CD229 and CD244. CD48 is found on the surface of lymphocytes and other immune cells, dendritic cells and endothelial cells, and participates in activation and differentiation pathways in these cells. CD48 was the first B-cell-specific cellular differentiation antigen identified in transformed B lymphoblasts.

CD73, also known as ecto-5′-nucleotidase, is an enzyme that in humans is encoded by the NT5E gene.CD73 commonly serves to convert AMP to adenosine.The enzyme consists of a dimer of 2 identical 70-kD subunits bound by a glycosyl phosphatidyl inositol linkage to the external face of the plasma membrane. The enzyme is used as a marker of lymphocyte differentiation. A  deficiency of CD73 occurs in a variety of immunodeficiency diseases.

CD73, also known as ecto-5′-nucleotidase, is an enzyme that in humans is encoded by the NT5E gene.CD73 commonly serves to convert AMP to adenosine.The enzyme consists of a dimer of 2 identical 70-kD subunits bound by a glycosyl phosphatidyl inositol linkage to the external face of the plasma membrane. The enzyme is used as a marker of lymphocyte differentiation. A  deficiency of CD73 occurs in a variety of immunodeficiency diseases.

CD96 (Cluster of Differentiation 96), also known as Tactile (T cell activation, increased late expression), is a receptor protein which is expressed on T cells and NK cells and shares sequence similarity with CD226 (also known as DNAM-1). The main ligand of CD96 is CD155 and CD96 competes with CD226 for binding to CD155. This protein belongs to the immunoglobulin superfamily and may play a role in the adhesive interactions of activated T and NK cells during the late phase of the immune response. It may also promote NK cell-target adhesion by interacting with PVR present on target cells and function in antigen presentation.

CD96 (Cluster of Differentiation 96), also known as Tactile (T cell activation, increased late expression), is a receptor protein which is expressed on T cells and NK cells and shares sequence similarity with CD226 (also known as DNAM-1). The main ligand of CD96 is CD155 and CD96 competes with CD226 for binding to CD155. This protein belongs to the immunoglobulin superfamily and may play a role in the adhesive interactions of activated T and NK cells during the late phase of the immune response. It may also promote NK cell-target adhesion by interacting with PVR present on target cells and function in antigen presentation.

CD96 (Cluster of Differentiation 96), also known as Tactile (T cell activation, increased late expression), is a receptor protein which is expressed on T cells and NK cells and shares sequence similarity with CD226 (also known as DNAM-1). The main ligand of CD96 is CD155 and CD96 competes with CD226 for binding to CD155. This protein belongs to the immunoglobulin superfamily and may play a role in the adhesive interactions of activated T and NK cells during the late phase of the immune response. It may also promote NK cell-target adhesion by interacting with PVR present on target cells and function in antigen presentation.

Molecular Formula : C34H43N3O3

Molecular Formula : C34H43N3O3

Molecular Formula : C32 H43 N O4

Molecular Formula : C32 H43 N O4

Molecular Formula : C32 H43 N O4

Molecular Formula : C14H11BrN4O3S

Molecular Formula : C5H11ClN3Pt . Cl

Molecular Formula : C5H11ClN3Pt . Cl

Molecular Formula : C5H11ClN3Pt . Cl

Carcinoembroyonic antigen (CEA) is a glycoprotein, produced during the embryonic and fetal period. The high concentration of CEA in blood are observed in many patients with cancer of the lung, liver, pancreas, breast, colon and prostate. The elevated CEA levels are related to the stage of the disease.

Carcinoembroyonic antigen (CEA) is a glycoprotein, produced during the embryonic and fetal period. The high concentration of CEA in blood are observed in many patients with cancer of the lung, liver, pancreas, breast, colon and prostate. The elevated CEA levels are related to the stage of the disease.

Carcinoembroyonic antigen (CEA) is a glycoprotein, produced during the embryonic and fetal period. The high concentration of CEA in blood are observed in many patients with cancer of the lung, liver, pancreas, breast, colon and prostate. The elevated CEA levels are related to the stage of the disease.

Carcinoembroyonic antigen (CEA) is a glycoprotein, produced during the embryonic and fetal period. The high concentration of CEA in blood are observed in many patients with cancer of the lung, liver, pancreas, breast, colon and prostate. The elevated CEA levels are related to the stage of the disease.

Carcinoembroyonic antigen (CEA) is a glycoprotein, produced during the embryonic and fetal period. The high concentration of CEA in blood are observed in many patients with cancer of the lung, liver, pancreas, breast, colon and prostate. The elevated CEA levels are related to the stage of the disease.

Carcinoembroyonic antigen (CEA) is a glycoprotein, produced during the embryonic and fetal period. The high concentration of CEA in blood are observed in many patients with cancer of the lung, liver, pancreas, breast, colon and prostate. The elevated CEA levels are related to the stage of the disease.

Carcinoembryonic antigen (CEA) also known as Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), CD antigen CD66e, Meconium antigen 100, is an oncofetal glycoprotein that is normally expressed by mucosal cells. CEA is a member of the immunoglobulin (Ig) superfamily of proteins. CEA is a glycophosphatidylinositol- (GPI-) linked membrane-anchoring protein that is exposed to the cell surface that faces the extracellular matrix. The membrane-anchoring region of CEA can be cleaved by phospholipase C and phospholipase D. The cleaved products are soluble and circulating through blood vessels. Thus, CEA can be present as secreted and cell surface-anchored forms. CEA is functionally associated with cellular interaction, cell adhesion, immune response, anoikis resistance, and promotion of liver metastasis. CEA overexpression is associated with many types of cancers including gastrointestinal, respiratory, and genitourinary system and breast cancers.

Carcinoembryonic antigen (CEA) also known as Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), CD antigen CD66e, Meconium antigen 100, is an oncofetal glycoprotein that is normally expressed by mucosal cells. CEA is a member of the immunoglobulin (Ig) superfamily of proteins. CEA is a glycophosphatidylinositol- (GPI-) linked membrane-anchoring protein that is exposed to the cell surface that faces the extracellular matrix. The membrane-anchoring region of CEA can be cleaved by phospholipase C and phospholipase D. The cleaved products are soluble and circulating through blood vessels. Thus, CEA can be present as secreted and cell surface-anchored forms. CEA is functionally associated with cellular interaction, cell adhesion, immune response, anoikis resistance, and promotion of liver metastasis. CEA overexpression is associated with many types of cancers including gastrointestinal, respiratory, and genitourinary system and breast cancers.

Carcinoembryonic antigen (CEA) also known as Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), CD antigen CD66e, Meconium antigen 100, is an oncofetal glycoprotein that is normally expressed by mucosal cells. CEA is a member of the immunoglobulin (Ig) superfamily of proteins. CEA is a glycophosphatidylinositol- (GPI-) linked membrane-anchoring protein that is exposed to the cell surface that faces the extracellular matrix. The membrane-anchoring region of CEA can be cleaved by phospholipase C and phospholipase D. The cleaved products are soluble and circulating through blood vessels. Thus, CEA can be present as secreted and cell surface-anchored forms. CEA is functionally associated with cellular interaction, cell adhesion, immune response, anoikis resistance, and promotion of liver metastasis. CEA overexpression is associated with many types of cancers including gastrointestinal, respiratory, and genitourinary system and breast cancers.

Carcinoembryonic antigen (CEA) also known as Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), CD antigen CD66e, Meconium antigen 100, is an oncofetal glycoprotein that is normally expressed by mucosal cells. CEA is a member of the immunoglobulin (Ig) superfamily of proteins. CEA is a glycophosphatidylinositol- (GPI-) linked membrane-anchoring protein that is exposed to the cell surface that faces the extracellular matrix. The membrane-anchoring region of CEA can be cleaved by phospholipase C and phospholipase D. The cleaved products are soluble and circulating through blood vessels. Thus, CEA can be present as secreted and cell surface-anchored forms. CEA is functionally associated with cellular interaction, cell adhesion, immune response, anoikis resistance, and promotion of liver metastasis. CEA overexpression is associated with many types of cancers including gastrointestinal, respiratory, and genitourinary system and breast cancers.

Carcinoembryonic antigen (CEA) also known as Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), CD antigen CD66e, Meconium antigen 100, is an oncofetal glycoprotein that is normally expressed by mucosal cells. CEA is a member of the immunoglobulin (Ig) superfamily of proteins. CEA is a glycophosphatidylinositol- (GPI-) linked membrane-anchoring protein that is exposed to the cell surface that faces the extracellular matrix. The membrane-anchoring region of CEA can be cleaved by phospholipase C and phospholipase D. The cleaved products are soluble and circulating through blood vessels. Thus, CEA can be present as secreted and cell surface-anchored forms. CEA is functionally associated with cellular interaction, cell adhesion, immune response, anoikis resistance, and promotion of liver metastasis. CEA overexpression is associated with many types of cancers including gastrointestinal, respiratory, and genitourinary system and breast cancers.

Carcinoembryonic antigen (CEA) also known as Carcinoembryonic antigen-related cell adhesion molecule 5 (CEACAM5), CD antigen CD66e, Meconium antigen 100, is an oncofetal glycoprotein that is normally expressed by mucosal cells. CEA is a member of the immunoglobulin (Ig) superfamily of proteins. CEA is a glycophosphatidylinositol- (GPI-) linked membrane-anchoring protein that is exposed to the cell surface that faces the extracellular matrix. The membrane-anchoring region of CEA can be cleaved by phospholipase C and phospholipase D. The cleaved products are soluble and circulating through blood vessels. Thus, CEA can be present as secreted and cell surface-anchored forms. CEA is functionally associated with cellular interaction, cell adhesion, immune response, anoikis resistance, and promotion of liver metastasis. CEA overexpression is associated with many types of cancers including gastrointestinal, respiratory, and genitourinary system and breast cancers.