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Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

Recombinant Fatty Acid Binding Protein is a newly introduced plasma marker of acute myocardial infarction (AMI). The plasma kinetics of FABP (15kD) closely resemble those of myoglobin in that elevated plasma concentrations are found within 2 hours after AMI and return to normal generally within 18 to 24 hours. But the concentration of FABP in the skeletal muscle is 20 times lower than in cardiac tissue (for myoglobin the same content for cardiac and skeletal tissue), that makes FABP to be more cardiac specific than myoglobin. This makes FABP a useful biochemical marker for the early assessment or exclusion of AMI. FABP also appears to be a useful plasma marker for the estimation of myocardial infarct size.

EPO is a member of the EPO/TPO family and encodes a secreted, glycosylated cytokine composed of 4 alpha helical bundles. EPO is found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. EPO also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types.

SERPINB5 (Maspin) is a tumor suppressor protein of the serine proteinase inhibitor family. Maspin plays a vital role in embryonic development through critical functions in cell adhesion. In addition, Maspin is present in normal breast and prostatic epithelial cells although down regulated in the particular carcinomas. SERPINB5 impedes the growth, invasion, and metastatic properties of mammary tumors as well as the invasive ability of pancreatic ductal adenocarcinoma cells. SERPINB5 being a breast tumor suppressor gene is a significant marker of the disease progression in breast neoplasms. Furthermore, high expression of maspin is linked to squamous cell carcinoma in non-small-cell lung cancer. Moreover, maspin expression has been directly linked with the biological aggressiveness of ovarian carcinoma. Maspin exhibits no serine protease inhibitory activity since it does not undergo the stressed to relaxed conformational transition typical of active serpins.

Interleukin 13 Receptor, Alpha 2 (IL13RA2) is a member of the type I cytokine receptor family, Type 5 subfamily. IL13RA2 is related to l13RA1, a subunit of the interleukin 13 receptor complex. IL13RA2 binds IL13 with high affinity, though lacking the cytoplasmic domain, and does not appear to function as a signal mediator. IL13RA2 plays a role in the internalization of IL13.

The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.

S100A11 is a member of the S100 family of proteins which contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100A11 may function in motility, invasion and tubulin polymerisation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of S100A11 have been implicated in tumor metastasis.

IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.

IL-17 family members are glycoproteins secreted as dimers which induce local cytokine production and recruit granulocytes to sites of inflammation. The IL-17 family is comprised of at least six pro-inflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 is induced by IL-15 and IL-23, mostly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL17B Diseases associated with IL17B include spondyloarthropathy, and neuronitis, and among its related super-pathways are Mucin expression in CF via IL-6, IL-17 signaling pathways and STAT3 Pathway.

Maltose Binding Protein (MBP) is a part of the maltose/maltodextrin system of Eschericia coli bacteria, which is responsible for the uptake and efficient catabolism of maltodextrins. It is a complex regulatory and transport system involving many proteins and protein complexes.
Maltose binding protein MalE,MBP, is part of the maltodextrin transport system in E. coli. The maltodextrins diffuse through the LamB pore located in the outer membrane into the periplasm. The sugar is bound to MalE which prevents it to diffuse back outside. MalE passes the sugar to a complex of MalF and MalG in the cytoplasmic membrane where active tranport is mediated by the ATPase MalK. MBP molecular weight is 40,622 dalton. There are two domains in the protein with similar secondary structure (central pleated sheets are surrounded by helices) . The domains are connected by three bridges, between the domains is a deep groove in which the sugar is bound. All hydroxyl groups of the sugar are fixed by sidechains of the protein by hydrogen bonds. Some water molecules are part of the hydrogen bridge network.

Interleukin-23 receptor (IL23R) is a member of the type I cytokine receptor family, Type 2 subfamily. IL23R contains two fibronectin type-III domains and is expressed by monocytes, Th1, Th0, NK and dendritic cells. IL23R protein pairs with the receptor molecule IL12RB1/IL12Rbeta1, and both are necessary for IL23A signaling. IL23R protein associates constitutively with JAK2 (Janus kinase 2), and it also binds to transcription activator STAT3 in a ligand-dependent manner. IL23R binds IL23 and mediates T-cells, NK cells and perhaps certain macrophage/myeloid cells stimulation most likely by way of activation of the Jak-Stat signaling cascade. IL23R might be responsible for autoimmune inflammatory diseases and be vital for tumorigenesis.

CD37 belongs to the transmembrane 4 superfamily, otherwise known as the tetraspanin family. Most of its members are cell-surface proteins which are distinguished by the presence of 4 hydrophobic domains. These proteins mediate signal transduction events which have a role in the regulation of cell development, activation, growth and motility. CD37 protein is a cell surface glycoprotein which is known to form complexes with integrins and other transmembrane 4 superfamily proteins. CD37 may also havea role in T-cell-B-cell interactions.

Calpain, Small Subunit 1 (CAPNS1) belongs to the calpain small subunit family. Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases, widely distributed in mammalian cells. Calpain families are implicated in neurodegenerative processes, considering that their activation can be triggered by calcium influx and oxidative stress. Calpains function as heterodimers, comprising a specific large catalytic subunit (calpain 1 subunit in Calpain I, and calpain 2 subunit in Calpain II), and a common small regulatory subunit encoded by the CAPNS1 gene. The CAPNS1 protein is vital for the stability and function of both calpain heterodimers, whose proteolytic activities influence numerous cellular functions including apoptosis, proliferation, migration, adhesion, and autophagy.

Interleukin-6 Signal Transducer or IL6ST is a receptor, part of the family of class 1 cytokine receptor. IL6ST binds to IL-6 through membrane-anchored or soluble IL-6R starts a connection between another complex of IL6ST and IL-6 , thus forming a homo-dimer and a signal transduction occurs.

TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.

The IL1RL1 gene is a member of the IL-1 receptor family, encoding a transmembrane protein with a structure similar to IL-1R1. IL1RL1 is a receptor for interleukin-33, its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. IL1RL1 may possibly be involved in helper T-cell function. IL1RL1 is highly expressed in kidney, lung, placenta, stomach, skeletal muscle, colon and small intestine.A soluble form of the IL1RL1 is produced from the same gene by alternative splicing and was shown to be expressed in several cell types including fibroblasts and mast cells. Soluble IL1RL1 also acts as a negative regulator of Th2 cytokine production and high levels have been reported in several disease states and conditions including asthma, sepsis and myocardial infarction.Analysis of the similar gene in mouse suggested that the IL1RL1 receptor can be induced by proinflammatory stimuli, and may be involved in the function of helper T cells.

SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.

NFATC2, also known as nuclear factor of activated T-cells 2, belongs to the nuclear factor of activated T cells family. NFATC2 takes a significant part in the course of T helper cell differentiation, activation, and effector function. Even though KO of an individual NFAT isoform in T cells directs to rather minor effects, T cells lacking for NFATC1 and 2 totally fail to produce T helper cell effector cytokines, for instance the interleukins IL-4 and IL-2. Moreover, NFATC2 is highly phosphorylated and kept in the cytoplasm. Next T cell receptor stimulation, dephosphorylation via calcium-activated calcineurin induces a conformational modification of NFATC2 which reveals a few nuclear localization sequences.

Human IL-36a belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. IL-36a is an 18-22kDa, 158aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential from N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
Human IL-36a (aa 6-158) shares 57-68% aa sequence homology with mouse, rabbit, equine and bovine IL-36a and 27-57% aa sequence homology with other new IL-1 family members. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.

Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

Human immunodeficiency virus (HIV) is a retrovirusthat can lead to a condition in which the immune systembegins to fail, leading to opportunistic infections. HIV primarily infects vital cells in the humanimmune systemsuch as helper T cells(specifically CD4+ T cells), macrophagesand dendritic cells. HIV infection leads to low levels of CD4+ T cells through three main mechanisms: firstly, direct viral killing of infected cells; secondly, increased rates of apoptosisin infected cells; and thirdly, killing of infected CD4+ T cells by CD8 cytotoxic lymphocytesthat recognize infected cells. When CD4+ T cell numbers decline below a critical level, cell-mediated immunityis lost, and the body becomes progressively more susceptible to opportunistic infections. HIV was classified as a member of the genus Lentivirus, part of the family of Retroviridae. Lentiviruses have many common morphologies and biological properties. Many species are infected by lentiviruses, which are characteristically responsible for long-duration illnesses with a long incubation period. Lentiviruses are transmitted as single-stranded, positive-sense, enveloped RNA viruses. Upon entry of the target cell, the viral RNA genomeis converted to double-stranded DNAby a virally encoded reverse transcriptasethat is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integraseso that the genome can be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latentand the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated that can then infect other cells.

IL-17 family members are glycoproteins secreted as dimers which induce local cytokine production and recruit granulocytes to sites of inflammation. The IL-17 family is comprised of at least six pro-inflammatory cytokines that share a conserved cysteine-knot structure but diverge at the N-terminus. IL-17 is induced by IL-15 and IL-23, mostly in activated CD4+ T cells distinct from Th1 or Th2 cells. IL-17B binds the IL-17B receptor, but not the IL-17 receptor; it is most homologous with IL-17D, which is expressed by resting CD4+ T cells and CD19+ B cells. IL17B Diseases associated with IL17B include spondyloarthropathy, and neuronitis, and among its related super-pathways are Mucin expression in CF via IL-6, IL-17 signaling pathways and STAT3 Pathway.

Influenza A virus subtype H5N1 is a subtype of the Influenza A virus. Subtype H5N1 is commonly known as avian influenza or bird flu. H5N1 may cause more than one influenza pandemic as it is expected to continue mutating in birds. The dominant strain of HPAI A (H5N1) evolved creating the Z genotype. It has also been called Asian lineage HPAI/A/H5N1 which is divided into 2 antigenic clades. "Clade 1 includes human and bird isolates from Vietnam, Thailand, and Cambodia and bird isolates from Laos and Malaysia. Clade 2 viruses were first identified in bird isolates from China, Indonesia, Japan, and South Korea before spreading westward to the Middle East, Europe, and Africa.