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Killer cell immunoglobulin-like receptor 2DL4, also known as KIR2DL4 is part of the killer cell Ig-like receptor (KIR) family. KIR proteins with the long cytoplasmic domain transduce inhibitory signals through an immune tyrosine-based inhibitory motif (ITIM), whereas KIR proteins which contain the short cytoplasmic domain, lack the ITIM motif and as a substitute associate with the TYRO protein tyrosine kinase binding protein to transduce activating signals. KIR2DL4 stimulates NK cells to produce IFN-gamma and stimulation with IL-2 upregulates cell surface expression on CD56dimcells and leads to the inhibition of the cytolytic NK cell function.

TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

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.

Anthrax PA (Protective Antigen) and Anthrax LF (Lethal Factor), along with Anthrax EF (Edema Factor), are toxins produced by Bacillus anthracis. All three of the proteins must be present for toxicity to occur. It begins with the binding of PA to its cell-surface receptor, ATR (Anthrax Toxin Receptor), at which point PA is cleaved and the resulting 63 kD carboxyl-terminal fragment binds to LF and EF. LF is a protease that is known to cleave members of the mitogen-activated protein kinase kinase (MAPKK) family(2).

CD9 which is found on the surface of exosomes is a cell surface glycoprotein which is interacts with integrins and various transmembrane superfamily proteins. CD9 is involved in platelet activation and aggregation and also regulates paranodal junction formation. CD9 takes part in cell adhesion and migration and also promotes muscle cell fusion. CD9 is necessary for the egg-sperm fusion during mammalian fertilization.

Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

Interleukin-27 protein is related to IL-12A & is one of the subunits of a heterodimeric cytokine complex. IL-27 interacts with EBV induced gene 3 also called EBI3, and forms a complex that drives rapid expansion of CD4 (+) T cells. IL-27 complex is synergizes with IL-12 in order to trigger the cytokine production of IFN-Gamma of CD4 (+) T cells. The biological effect of IL-27 is mediated by class-I cytokine receptor (WSX1/TCRR). The pro-inflammatory activity of IL-27 is mediated through the growing expression of key molecules involved in the MHC class-I & MHC class-II pathways. Both MHC class-I and MHC-class-II expression are increased in endothelial cells after Interleukin-27 stimulation which suggests that it may play an important role in conferring the immune function on vascular endothelium IL-27p28 subunit can be induced by IFN-beta and during LPS-induced maturation of dendritic cells in type-I IFN-dependent manner through IFN regulatory factor-1 activation. Interleukin-27 regulates Interleukin-12 responsiveness of CD4+ T cells through Stat1-dependent and -independent mechanisms. IL-17 & IL-23 play an important IL-17 role in inflammation. Interleukin-27 possesses potent anti-angiogenic activity that plays an important role in its antitumor and antimetastatic activities. EBV induced gene 3 plays a role, independently from IL-27, in regulating anti-viral or anti-tumoral immune responses. Interleukin-27 is a potent inhibitor of HIV-1 replication in macrophages, CD4+ T cells, peripheral blood mononuclear cells. Interleukin-27 triggers STAT activation and gene transcription.

Troponin I (TnI), troponin T (TnT) and troponin C (TnC) form the troponin complex of the thin filaments of striated muscle. TnI is acts as the inhibitory subunit by blocking actin-myosin interactions and thereby mediating striated muscle relaxation. The TnI subfamily contains 3 genes: TnI-skeletal-fast-twitch, TnI-skeletal-slow-twitch, and TnI-cardiac. The TNNI3 gene encodes the TnI-cardiac protein and is exclusively expressed in cardiac muscle tissues. Mutations in the TNNI3 gene cause familial hypertrophic cardiomyopathy type 7 (CMH7) and familial restrictive cardiomyopathy (RCM).

A fusion tag called FLAG consists of eight amino acids (AspTyrLysAspAspAspAspLys) including an enterokinase-cleavage site. FLAG is specifically designed for immunoaffinity chromatography. It allows elution under non-denaturing conditions. Several antibodies against this peptide have been developed. One antibody. denoted as M1. binds the peptide in the presence of bivalent metal cations. preferably Ca(+). Elution is effected by chelating agents. Another strategy is competitive elution with excess of free Flag Peptide.
The FLAG peptide purifies and detects recombinant fusion proteins. FLAG peptide is useful in Western blotting, immunocytochemistry, immunoprecipitation, flow cytometry, protein purification, and in the study of protein-protein interactions, cell ultrastructure, and protein localization. Flag peptide is a hydrophilic tag which significantly improves the detection and purification of recombinant fusion proteins.

Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.

Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.

AURKA (Aurora Kinase A) belongs to the mitotic serine/threonine kinases family. AURKA is a cell cycle-regulated kinase which may be involved in microtubule formation and/or stabilization at the spindle pole during chromosome segregation. AURKA is found at the centrosome in interphase cells and at the spindle poles in mitosis. Since the AURKA expression is cell-cycle regulated, it is low in G1/S, it accumulates during G2/M, and it decreases rapidly after. AURKA is involved in important processes during mitosis and meiosis whose proper function is essential for healthy cell proliferation. In addition, AURKA plays an essential role in tumourigenesis and is overexpressed in various types of cancers. AURKA is strongly expressed in the testis, colon, ovarian, prostate, neuroblastoma, breast and cervical cancer cell lines and weakly in skeletal muscle, thymus and spleen. AURKA interacts with its substrates BORA and ARHGEF2, as well as with TACC1 and CPEB1.
Defects in the AURKA gene cause numerical centrosome aberrations including aneuploidy. AURKA overexpression has been linked to chromosomal instability in colorectal cancer. AURKA expression may have a prognostic significance in ovarian carcinoma.

MAT2A is an important enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP. MAT2A is expressed in extrahepatic tissues. In liver, MAT2A expression associates with growth, dedifferentiation, and cancer. NF-kappa B and AP-1 are necessary for basal MAT2A expression in HepG2 cells and mediate the increase in MAT2A expression in response to TNF-alpha. Up-regulation of MAT2A provides growth improvement and s-adenosylmethionine and methylthioadenosine thus can block mitogenic signaling in colon cancer cells. Lower expression of both MAT2A and MAT2beta and interfere with leptin signaling in liver cancer cells.

CCL3L1 is a small cytokine that belongs to the CC chemokines. The CCL3L1 gene is one of several cytokine genes clustered on the q-arm of chromosome 17. CCL3L1 is involved in immunoregulatory and inflammatory processes. CCL3L1 binds to several chemokine receptors including CCBP2 and CCR5. CCR5 is a co-receptor for HIV, and binding of the CCL3L1 protein to CCR5 inhibits HIV entry.

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.
The three Ig-domain from of inhibitory killer cell Ig-like receptor 1(KIR3DL1, NKB1, nkat3, p70KIR) is a NK cell receptor for polymorphic HLA-B determinant. KIR3DLl recognizes the Bw4 determinant defined by sequence motifs at positions 77-83 of the HLA-B heavy chain. The cytoplasmic tail of KIR, which contains two immunoreceptor tyrosine-based inhibition motifs (ITIMs), mediates inhibitory signal transduction that prevents killer cell-mediated cytotoxicity. A His-tag fusion protein of KIR3DL1 cytoplasmic tail (361-444aa) was overexpressed as insoluble protein aggregates (inclusion bodies).

QPRT is a key enzyme in the catabolism of quinolinate. QPRT is in between the tryptophannicotinamide adenine dinucleotide (NAD) pathway, resulting in the production of nicotinic acid, carbon dioxide and pyrophosphate. Rise of QPRT levels in the brain is related to the pathogenesis of neurodegenerative disorders such as epilepsy, Alzheimer's disease, and Huntington's disease.

Phosphopantothenate-cysteine ligase (PPCS) catalyzes the first step in the biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5), which is a vital universal pathway in prokaryotes and eukaryotes. PPCS, being one of the last enzymes in this pathway, converts phosphopantothenate to phosphopantothenoylcysteine.

Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

N-Acetylglucosamine Kinase (NAGK) is a part of the eukaryotic-type N-acetylglucosamine kinase family. NAGK transforms endogenous N-acetylglucosamine (GlcNAc), a main component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. NAGK is a significant salvage enzyme of amino sugar metabolism in mammals which has ManNAc kinase activity.

GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

CD4 is a cell-surface glycoprotein found on the mature helper T cells and immature thymocytes, as well as on monocytes and macrophages. (Some cytotoxic T cells have CD4 protein as well.) Normally, about 65% of T cells in the blood are CD4+ (have CD4 protein protruding from their membrane). A mature T cell with either have CD4 or CD8, but not both. During one stage of development T cells develop CD4 and CD8 receptors, but they eventually are differentiated in the thymus and become more specialized.

IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis.