"PROSCI"

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The exact function of C6orf140 remains unknown.

Supplier: PROSCI

The exact function of C9orf46 remains unknown.

Supplier: PROSCI

The exact function of C9orf46 remains unknown.

Supplier: PROSCI

Heparan sulfate proteoglycans (HSPGs) act as coreceptors for numerous heparin-binding growth factors and cytokines and are involved in cell signaling. Heparan sulfate 6-O-endosulfatases, such as SULF2, selectively remove 6-O-sulfate groups from heparan sulfate. This activity modulates the effects of heparan sulfate by altering binding sites for signaling molecules.Heparan sulfate proteoglycans (HSPGs) act as coreceptors for numerous heparin-binding growth factors and cytokines and are involved in cell signaling. Heparan sulfate 6-O-endosulfatases, such as SULF2, selectively remove 6-O-sulfate groups from heparan sulfate. This activity modulates the effects of heparan sulfate by altering binding sites for signaling molecules (Dai et al., 2005 [PubMed 16192265]).

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PCDHAC2 is a potential calcium-dependent cell-adhesion protein. It may be involved in the establishment and maintenance of specific neuronal connections in the brain.This gene is a member of the protocadherin alpha gene cluster, one of three related gene clusters tandemly linked on chromosome five that demonstrate an unusual genomic organization similar to that of B-cell and T-cell receptor gene clusters. The alpha gene cluster is composed of 15 cadherin superfamily genes related to the mouse CNR genes and consists of 13 highly similar and 2 more distantly related coding sequences. The tandem array of 15 N-terminal exons, or variable exons, are followed by downstream C-terminal exons, or constant exons, which are shared by all genes in the cluster. The large, uninterrupted N-terminal exons each encode six cadherin ectodomains while the C-terminal exons encode the cytoplasmic domain. These neural cadherin-like cell adhesion proteins are integral plasma membrane proteins that most likely play a critical role in the establishment and function of specific cell-cell connections in the brain. Alternative splicing has been observed and additional variants have been suggested but their full-length nature has yet to be determined.

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Interleukin 37 (IL-37) is a member of the interleukin 1 cytokine family. It can bind to, and may be a ligand for interleukin 18 receptor (IL18R1/IL-1Rrp). IL-37 also binds to interleukin 18 binding protein (IL18BP), an inhibitory binding protein of interleukin 18 (IL18), and subsequently forms a complex with IL18 receptor beta subunit, and through which it inhibits the activity of IL18. IL-37 can also interact with Smad3 and expression of IL-37 in macrophages or epithelial cells resulted in near complete suppression of pro-inflammatory cytokines, suggesting that IL-37 may act as a natural suppressor of the innate inflammatory and immune responses.

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Omentin (Intelectin-1) is highly expressed in omental adipose tissue, small intestine and various other tissues. Omentin has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. It increases AKT phosphorylation in the absence and presence of insulin. It was suggested to play a role in the defence system against microorganisms by recognising carbohydrate chains of pathogens and bacterial components containing galactofuranosyl residues.

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IL-1RL2 is a member of the interleukin 1 receptor family, but it is incapable of binding to interleukin 1 alpha and interleukin 1 beta with high affinity. Together with IL-1RAcP, it can bind members of the IL-36 cytokine family, leading to activation of the NF-kappaB pathway. IL-1RL2 can also bind to IL-1F10, resulting in a decreased product of Th17 cytokines in response to immunological or LPS challenge, suggesting that one potential role of IL-1RL2 may be to modulate the immune and inflammation response.

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RANKL is an osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T cell proliferation. Important regulator of interactions between T cells and dendritic cells and may play a role in the regulation of the T cell-dependent immune response. RANKL plays an important role in the progression of Breast cancer.

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The cytokine IL-1 is responsible for initiating a variety of activities through the activation of transcription factors, NF-kappa B and AP-1, thereby promoting host response to injury or infection. IL-1F10 (Interleukin-1 family member 10), also known as FIL1T, IL1HY2 or FKSG75, is highly expressed in the skin, spleen and proliferating B-cells of the tonsil. IL-1F10 binds soluble IL-1 receptor type 1, and is one of nine Interleukin 1 families clustered on chromosome 2, where it is thought to participate in the regulation of adapted and innate immune responses. IL-1F10 and IL-1RN polymorphisms may play an important role in the susceptibility to developing rheumatoid arthritis.

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CD137 (4-1BB) is a member of the tumor necrosis factor (TNF) receptor family. CD137 is expressed by activated T cells, dendritic cells, NK cells, granulocytes and cells of blood vessel walls at sites of inflammation. CD137 has costimulatory activity for activated T cells. Crosslinking of CD137 enhances T cell proliferation, IL-2 secretion survival and cytolytic activity. CD137 was shown to enhance immune activity to eliminate tumours in mice.

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IL-36A is is a member of the interleukin 1 cytokine family whose gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2. IL-36A is thought to activate the NF-kappaB pathway through IL-1 receptor family members IL-1RL2 and IL-1RAcP. Like the related proteins IL-36B and IL-36G, IL-36A requires post-translational processing for full agonist activity, but the cleavage mechanism is currently unknown. The IL-36 cytokines have been suggested to amplify Th1 responses by enhancing proliferation and Th1 polarization of naive CD4+ T cells.

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Angiocidin shows sequence similarity with proteasome components and is also being referred to as 26A proteasome regulatory subunit S5A. Angiocidin shows both matrix and cytoplasmic distribution. It binds to thrombospondin-1 and alpha2beta1 integrin, and it inhibits tumour progression and angiogenesis. Angiocidin is expressed in various types of cancer, such as hepatocellular carcinoma, prostate, lung, bladder, and melanoma cancers.

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IL-36B is is a member of the interleukin 1 cytokine family whose gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2. IL-36B is thought to activate the NF-kappaB pathway through IL-1 receptor family members IL-1RL2 and IL-1RAcP. Like the related proteins IL-36A and IL-36G, IL-36B requires post-translational processing for full agonist activity, but the cleavage mechanism is currently unknown. The IL-36 cytokines have been suggested to amplify Th1 responses by enhancing proliferation and Th1 polarization of naive CD4+ T cells.

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DR6 is an orphan TNF receptor superfamily member belonging to a subgroup of receptors called death receptors. Expressed ubiquitously with high expression in lymphoid organs, heart, brain, and pancreas. Broadly expressed by developing neurons where it functions as pro-apoptotic factor. Recently, it has been reported that interaction with the beta-amyloid precursor protein (APP) activates a widespread caspase-dependent self-destruction program dependent on caspase-6.

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IL-36G is is a member of the interleukin 1 cytokine family whose gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2. IL-36G is thought to activate the NF-kappaB pathway through IL-1 receptor family members IL-1RL2 and IL-1RAcP. Like the related proteins IL-36A and IL-36B, IL-36G requires post-translational processing for full agonist activity, but the cleavage mechanism is currently unknown. IL-36G expression is stimulated by interferon-gamma, tumor necrosis factor-alpha and interleukin 1. The IL-36 cytokines have been suggested to amplify Th1 responses by enhancing proliferation and Th1 polarization of naive CD4+ T cells.