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TREM1 is a transmembrane receptor protein that is involved in monocytic activation and in the inflammatory response. TREM1 is expressed on the surface of neutrophils, mature monocytes and macrophages. TREM1 stimulates neutrophil and monocyte-mediated inflammatory responses. TREM1 also triggers the release of pro-inflammatory chemokines and cytokines, as well as increased surface expression of cell activation markers. Furthermore, TREM1 is an amplifier of inflammatory responses that are triggered by bacterial and fungal infections and is a fundamental mediator of septic shock. The expression of the soluble form of TREM1 increases during sepsis and can consequently be used as a biological marker for septic shock. TREM1 is strongly expressed in acute inflammatory lesions caused by bacteria and fungi. Increased TREM1 expression on monocytes is related to both infectious and noninfectious inflammatory processes.
TREM1 is vastly expressed in adult liver, lung and spleen than in corresponding fetal tissue. TREM1 is also expressed in the lymph node, placenta, spinal cord and heart tissues. TREM1 expression is more elevated in peripheral blood leukocytes than in the bone marrow and in normal cells than malignant cells. TREM1 is expressed at low levels in the early development of the hematopoietic system and in the promonocytic stage and at high levels in mature monocytes.

Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells.
The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes.
The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
KIR2DL1 is an inhibitory Killer Cell Ig-like Receptor (KIR, previously called p58 KIR, p58.1, cl-42, NKAT1, or KIR-K6), which recognizes class I MHC molecules (HLA-Cw2, -Cw4, -Cw5, and Cw6). The extracellular domain of KIR2DL1 was over expressed as insoluble protein aggregates (inclusion bodies).

SSR4 is a member of the TRAP-delta family. SSR4 is the delta subunit of the translocon-associated protein complex that participates in translocating proteins through the endoplasmic reticulum membrane. SSR4 positioned in the Xq28 region and organized in a compact head-to-head manner with the isocitrate dehydrogenase 3 (NAD+) gamma gene. Both genes are motivated by a CpG-embedded bidirectional promoter.

Low affinity immunoglobulin gamma Fc region receptor III-A (FCGR3A) is a receptor for the Fc portion of immunoglobulin G, and is involved in the elimination of antigen-antibody complexes from the circulation, as well as other antibody-dependent responses. FCGR3A needs to associate with the gamma subunit of Fc epsilon. The FCGR3A receptor is expressed on natural killer (NK) cells as an integral membrane glycoprotein anchored through a transmembrane peptide, while FCGR3B is expressed on polymorphonuclear neutrophils (PMN) where the receptor is anchored through a phosphatidylinositol (PI) linkage. In addition, FCGR3A is expressed on macrophages, subpopulation of T-cells, immature thymocytes and placental trophoblasts. FCGR3A mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis. FCGR3A gene mutations are linked with susceptibility to recurrent viral infections, susceptibility to systemic lupus erythematosus, and alloimmune neonatal neutropenia.

Shiga-like toxin (verotoxin) is a toxin produced by some strains of Escherichia coli. Shiga-like toxin is named for its similarity to the AB5-type Shiga toxin produced by the bacteria Shigella dysenteriae. There are two known types-SLT1 and SLT2. The Shiga-like toxin is linked with hemolytic-uremic syndrome. Shiga-like toxin requires highly specific receptors on the cells'' surface in order to attach and enter the cell. Species such as cattle, swine, and deer which do not carry these receptors may harbor toxigenic bacteria without any ill effect, dropping them in their feces, from where they may be distributed to humans. Shiga Like Toxin-1 Subunit B has nontoxic action, it is the functional region which binds to the receptor. The Shiga Like Toxin-1 Subunit B can be useful in vaccine study, antibody test and other functional research.

Interleukin-1 receptor type 1 (IL1R1) associates with the co-receptor IL1RAP to form the high affinity interleukin-1 receptor complex, which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. IL1R1 is a central mediator involved in numerous cytokine induced immune and inflammatory responses.

Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells. The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes. The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. KIR2DL3 is an inhibitory Killer Cell Ig-like Receptor (KIR, previously called p58 KIR, cl-6, NKAT2 or KIR-K7), which recognizes class I MHC molecules (HLA-Cw1, -Cw3, -Cw7, and Cw8). KIR2DL3 inhibits the activity of NK cells thus preventing cell lysis.

IL2-Ra is one of the three constituent subunits of the IL2 receptor. IL-2Ra is released into the serum after increased cellular expression such as increased activation of B and T cells. Clinical manifestations of IL2-Ra elevation include autoimmune conditions and some leukemias and lymphomas.

Killer-cell immunoglobulin-like receptors (KIRs), are a family of cell surface glycoproteins found on Natural Killer (NK) Cells, which are important cells of the immune system. They control the killing function of these cells by interacting with MHC class I molecules, which are expressed on all cell types. This interaction allows them to identify virally infected cells or tumor cells that have a distinctive low level of Class I MHC on their surface. The majority of KIRs are inhibitory, which means that their recognition of MHC suppresses the cytotoxic activity of their NK cell. Only a limited number of KIRs have the capacity to activate cells.
The KIR genes are found in a cluster on chromosome 19q13.4 within the 1 Mb leukocyte receptor complex (LRC). KIR molecules are extremely polymorphic, meaning their gene sequences differ significantly between individuals, so that different individuals have different arrays/repertoires of KIR genes.
The KIR proteins are categorized by the number of extracellular immunoglobulin domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain. KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM). Whereas KIR proteins with the short cytoplasmic domain lack the ITIM motif and instead associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals.
KIR2DS4 is an activating Killer Cell Ig-like Receptor (KIR, previously called p50 KIR, p50.3, cl39, or KAR-K1), which may recognize class I MHC molecules. KIR2DS4 does not inhibit the activity of NK cells.

Killer Cell lectin-Like Receptor Subfamily K, Member 1 (KLRK1) is an activating receptor which has recently generated considerable interest. The most fascinating of these, are a couple of closely related proteins known as MICA and MICB. These are cell-surface molecules distantly related to MHC class I proteins, and their genes have elements of heat shock promoters. Thus, MICA and MICB are expressed in the course of cell stress and are up-regulated in tumor cells and during viral infections. This receptor-ligand combination has a crucial role in the immune response to various pathologies.

Killer Cell lectin-Like Receptor Subfamily K, Member 1 (KLRK1) is an activating receptor which has recently generated considerable interest. The most fascinating of these, are a couple of closely related proteins known as MICA and MICB. These are cell-surface molecules distantly related to MHC class I proteins, and their genes have elements of heat shock promoters. Thus, MICA and MICB are expressed in the course of cell stress and are up-regulated in tumor cells and during viral infections. This receptor-ligand combination has a crucial role in the immune response to various pathologies.

Interleukin-2 Receptor Gamma (IL2RG) is a cytokine receptor sub-unit which is common to the receptor complexes for at least six different interleukin receptors. IL2RG is located on the surface of immature blood-forming cells in bone marrow. One end of the IL2RG protein resides outside of the cell where it binds to cytokines and the other end of the IL2RG protein resides in the interior of the cell where it transmits signals to the cell's nucleus. IL2RG teams up with other proteins to direct blood-forming cells to form lymphocytes. In addition, IL2RG directs the growth and maturation of lymphocyte subtypes, which kill viruses, make antibodies, and help regulate the entire immune system.

SSR is a glycosylated endoplasmic reticulum (ER) membrane receptor involved in protein translocation across the ER membrane. SSR is formed of 2 subunits, a 34-kD glycoprotein encoded by this gene and a 22-kD glycoprotein. SSR gene creates a number of mRNA species due to complex alternative polyadenylation. SSR is unique since it exploits arrays of polyA signal sequences which are mostly non-canonical.

Fas and Fas Ligand (FasL) are members of the TNF superfamily and are type I and type II transmembrane proteins, respectively. Binding of FasL to Fas initiates apoptosis in Fas-bearing cells. The apoptosis mechanism involves the recruitment of pro-caspase 8 through an adaptor molecule named FADD followed by processing of the pro-enzyme to active forms. These active caspases subsequently cleave a variety of cellular substrates leading to the eventual cell death. sFasR is able to inhibit FasL-induced apoptosis by acting as a decoy receptor whicht serves as a sink for FasL. The full length Fas Receptor is a 319 a.a type I transmembrane protein, which contains a 157 a.a extracellular domain, a 17 a.a transmembrane domain, and 145 a.a cytoplasmic domain. The mature human Fas ECD shares 55%, 58%, a.a sequence identity with the mouse, rat, Fas, respectively.

CCR6 belongs to the beta chemokine receptor family, which is predicted to be a 7 transmembrane protein similar to G protein-coupled receptors. CCR6 is preferentially expressed by immature dendritic cells and memory T cells. The ligand of CCR6 receptor is macrophage inflammatory protein 3 alpha (MIP-3 alpha). CCR6 receptor has been shown to be vital for B-lineage maturation and antigen-driven B-cell differentiation, and it may regulate the migration and recruitment of dentritic and T cells during inflammatory and immunological responses.

Killer Cell Immunoglobulin-Like Receptor, 3 Domains Long Cytoplasmic Tail 2 (KIR3DL2) is a type 1 transmembrane protein of the p70 family of killer cell Ig-like receptors. KIR3DL2 is a receptor on NK cells for HLA-A alleles which Inhibits their activity consequently preventing cell lysis.

TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene.

Anthrax toxin receptor 2, also known as ANTXR2, takes part in the configuration of little blood vessels (capillaries). ANTXR2 helps the toxin that leads to anthrax to attach to cells and trigger illness. ANTXR2 is necessary for cellular interactions with laminin and the extracellular matrix.

IL-21 is produced by CD4+ T cells in response to antigenic stimulation. Its action enhances antigen-specific responses of immune cells. The biological effects of IL-21 include induction of differentiation of T-cells-stimulated B-cells into plasma cells and memory B-cells, stimulation (in conjuction) with IL-4 of IgG production, and induction of apoptotic effects in na?ve B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the gamma chain (?c) found in other cytokine receptors including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3.

Since April 2012, cases of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) have been identified in various countries. Coronaviruses are the cause of the common cold, SARS (severe acute respiratory syndrome) and other severe illnesses with high mortality rates, all are classified into coronavirus family. MERS-CoV is a new type of SARS found in the coronavirus family causing severe pneumonia with sudden and serious respiratory illness with high mortality rates as well. Since January 27th 2015, the WHO has reported 956 human cases, including 351 deaths. More cases of the new coronavirus strain are expected. Like in other coronaviruses, large surface spike glycoprotein is a central structural protein of this virus; it is located above the virion surface to bind and enter into the target cell. Spike protein has 2 domains- S1 and S2. The S1 domain is responsible for cellular tropism and interaction with target cell, while the S2 domain is responsible for membrane fusion. The C-terminal of S1 domain contains a receptor binding domain, and is also a potential target for vaccine development and an antigen for diagnosis.

Interleukin-7 receptor (IL7R) ,is a hematopoietin receptor superfamily member. IL7R takes a vital part in lymphocyte differentiation, proliferation, multiple sclerosis, as well as survival. IL7R protein signaling is vital for T-cell development and regulation of native and memory T-cell homeostasis. Likewise, IL7R is critically needed for the proper function & development of lymphoid cells.