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Insulin-growth factor-like gene family is a new family of proteins consisting of four proteins in humans (IGFL1 to 4) and one in mice (mIGFL). mIGFL is expressed in normal skin in mice and further upregulated during inflammation responses in skin or after skin wounding. In human only IGFL1 expression is increased in psoriatic skin samples. mIGFL and human IGFL1 and 3 interact with specificity and high affinity to a novel receptor named IGF-like family receptor 1 (formerly TMEM-149). Analysis of the amino acid sequence of IGFLR1 indicated that this receptor is likely a novel member of the TNF-R family. IGFLR1 is expressed most abundantly on mouse T cells, suggesting that mIGFL and IGFL1 produced in the skin may potentially exert regulatory functions on T cell responses.

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ULK4 belongs to the Ser/Thr protein kinase superfamily and plays a role in the ATP-dependent phosphorylation of target proteins. Knockout of ULK genes results in a severe defect in the autophagy pathway. ULK4, like the other Unc-51-like kinases such as ULK1, ULK2 and ULK3, is highly conserved among eukaryotes. ULK4 has been implicated as a gene involved in the development of hydrocephalus. This neurologic disorder is being used in animal models to elucidate factors responsible for the excessive accumulation of cerebrospinal fluid in hydrocephalic humans.

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Insulin-growth factor-like gene family is a new family of proteins consisting of four proteins in humans (IGFL1 to 4) and one in mice (mIGFL). mIGFL is expressed in normal skin in mice and further upregulated during inflammation responses in skin or after skin wounding. In human only IGFL1 expression is increased in psoriatic skin samples. mIGFL and human IGFL1 and 3 interact with specificity and high affinity to a novel receptor named IGF-like family receptor 1 (formerly TMEM-149). Analysis of the amino acid sequence of IGFLR1 indicated that this receptor is likely a novel member of the TNF-R family. IGFLR1 is expressed most abundantly on mouse T cells, suggesting that mIGFL and IGFL1 produced in the skin may potentially exert regulatory functions on T cell responses.

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The CXCL12 protein, also known as SDF1, is a stromal cell-derived alpha chemokine member of the intercrine family. CXCL12 functions as the ligand for the G-protein coupled receptor, chemokine (C-X-C motif) receptor 4 (CXCR4) and CXCR7, and plays a role in many diverse cellular functions, including embryogenesis, immune surveillance, inflammation response, tissue homeostasis, and tumor growth and metastasis . Mutations in this gene are associated with resistance to human immunodeficiency virus type 1 infections.

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RANK (TRANCE-R; CD265) is the receptor for RANKL/TRANCE/OPGL. It is essential for RANKL-mediated osteoclastogenesis and is involved in the regulation of interactions between T cells and dendritic cells.

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Interleukin-22 (IL-22) is a cytokine important for the modulation of tissue responses during inflammation. Unlike the distantly related IL-10, IL-22 does not inhibit the production of proinflammatory cytokines in monocytes in response to LPS, but it has some inhibitory effects on IL-4 production from Th2 T cells. IL-22 is expressed by both the adaptive arm of the immune system such as CD4 T cell subsets including Th17 cells, as well as by innate lymphocytes such as NK and LTi-like cells. IL-22 is highly expressed in several chronic inflammatory conditions, and studies suggest that IL-22 plays both inflammatory and protective roles.

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LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities also include the induction of hematopoietic differentiation in normal and myeloid leukaemia cells, the induction of neuronal cell differentiation and the stimulation of acute-phase protein synthesis in hepatocytes. LIF activates JAK & STAT signalling in human embryonic stem (ES) cells, but this pathway does not maintain pluripotency in these cells, which instead rely on FGF2-mediated ERK signalling. By contrast, mouse ES cells can be maintained by LIF-mediated JAK & STAT signalling. LIF binds to a high affinity heterodimeric receptor complex consisting of two proteins: LIF-R alpha that binds LIF with low affinity and the 130kDa (gp130) subunit that by itself does not bind LIF, but is required for high affinity binding of LIF.

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Alpha-tubulin belongs to the tubulin superfamily, which is composed of six distinct families. Along with beta-tubulins, alpha-tubulins are the major components of microtubules. These microtubules are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintenance of cell shape. Alpha- and beta-tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22-nm diameter (reviewed in 1). Tyrosine ligase adds a C-terminal tyrosine to monomeric alpha-tubulin. Assembled microtubules can again be detyrosinated by a cytoskeleton-associated carboxypeptidase (2). Another post-translational modification of detyrosinated alpha-tubulin is C-terminal polyglutamylation, which is characteristic of microtubules in neuronal cells and the mitotic spindle (3). Like GAPDH and beta-Actin, this antibody makes an excellent loading control in immunoblots.

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TESPA1 is a critical component of the TCR signalosome and is essential for T cell selection and maturation through the regulation of TCR signaling during T cell development. TESPA1 encodes a protein of 458 amino acids and is highly conserved among vertebrate species. TESPA1 expression was tightly regulated during T cell development, with highest expression at the DP stage. TESPA1 deficiency resulted in failure of positive selection and substantially fewer of CD4+ and CD8+ SP cells in the thymus (1,4).

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Flagellin is the subunit protein which polymerises to form the filaments of bacterial flagella. It activates the innate immune system through the receptor Toll-like Receptor 5 (TLR5) and the intracellular protein NLRC4 (NLR family CARD domain-containing protein 4).

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The Dynamin-1-like protein (DNM1L) is a member of the dynamin superfamily of GTPases. DNM1L mediates mitochondrial and peroxisomal division, and is involved in developmentally regulated apoptosis and programmed necrosis. Dysfunction of this gene is implicated in several neurological disorders, including Alzheimer's disease. Mutations in this gene are associated with the autosomal dominant disorder, encephalopathy, lethal, due to defective mitochondrial and peroxisomal fission (EMPF).

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IL-36Ra/IL-1F5 is a highly and a specific antagonist of the IL-1 receptor-related protein 2-mediated response to IL-36alpha (IL-1F6), IL-36beta (IL-1F8) and IL-36gamma (IL-1F9). These cytokines bind to IL-36R (IL-1Rrp2) and IL-1RAcP, activating similar intracellular signals as IL-1. IL-36Ra inhibits the production of proinflammatory cytokines, including IL-12, IL-1beta, IL-6, TNF-alpha and IL-23 induced by IL-36 in BMDC and CD4 T cells. Skin and dendritic cells are target of the IL-36 interleukins leading to a Th1 response. Recently mutations that affect the levels and the activity of IL-36Ra have been found in patients with pustular psoriasis, leading to enhanced production of inflammatory cytokines (IL-8 in particular) by keratinocytes.

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The 40S ribosomal protein SA (RPSA) is a high-affinity, non-integrin family, laminin receptor, also known as 67 kDa laminin receptor or 37 kDa laminin receptor precursor (37LRP). Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes and have been implicated in a variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. RPSA is overexpressed in multiple types of cancers and has recently been shown to act as a cancer-specific death receptor.

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MED6 is a component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. And mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.

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TRIM9 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. Its function has not been identified. Alternate splicing of this gene generates two transcript variants encoding different isoforms.The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies. Its function has not been identified. Alternate splicing of this gene generates two transcript variants encoding different isoforms.

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NFRKB binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'.