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Bcl-2-like protein 2 (BCL2L2) belongs to the Bcl-2 family. BCL2L2 is highly expressed in thebrain, spinal cord, testis, pancreas, heart, spleen, and mammary glands. BCL2L2 is a peripheral membrane protein containing three motifs, BH1, BH2 and BH4. The BH4 motif appears to be involved in the anti-apoptotic function. The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. BCL2L2 promotes cell survival and blocks dexamethasone-induced apoptosis. Furthermore, BCL2L2 mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.

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BH3-Interacting Domain Death Agonist (BID) is a member of the Bcl-2 protein family which regulates outer mitochondrial membrane permeability. BID is a pro-apoptotic member that causes cytochrome c to be released from the mitochondria intermembrane space into the cytosol. Interaction of Bid with Bak causes altered mitochondrial membrane permeability. BID contains only the BH3 domain, which is required for its interaction with the Bcl-2 family proteins and for its pro-death activity. BID is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. It is an integrating key regulator of the intrinsic death pathway that amplifies caspase-dependent and caspase-independent execution of neuronal apoptosis. Therefore pharmacological inhibition of BID provides a promising therapeutic strategy in neurological diseases where programmed cell death is prominent, and also offer a new strategy for the treatment of acute renal failure associated with ischemia-reperfusion. BID receives direct inputs from a key regulator of the cell cycle arrest/DNA repair machinery (ATM), and therefore is an excellent candidate to coordinate genotoxic stress responses and apoptotic cell death. BID is a novel pro-apoptosis Bcl-2 family protein that is activated by caspase 8 in response to Fas/TNF-R1 death receptor signals. Deletion of BID inhibits carcinogenesis in the liver, although this genetic alteration promotes tumorigenesis in the myeloid cells. This is likely related to the function of BID to promote cell cycle progression into S phase. BID could be also involved in the maintenance of genomic stability by engaging at mitosis checkpoint.

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The Galectin family of proteins (with specificity for Nacetyllactosamine containing glycoproteins) consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). At least 14 mammalian galectins family members that share structural similarities in their carbohydrate recognition domains (CRD) have been identified to date. Unlike the selectin family of proteins, the carbohydrate binding specificity of galectins is calcium-independent. A common function of galectins is to cross-link structures containing N-acetyl-lactosamine located at the cell surface and within the extracellular matrix. They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins have been classified into the prototype galectins (1, 2, 5, 7, 10, 11, 13, 14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins (Galectin3) containing one CRD linked to a nonlectin domain, and the tandem repeat Galectins (4, 6, 8, 9, 12) consisting of two CRDs joined by a linker peptide. Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.

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The Galectin family of proteins, with specificity for Nacetyllactosaminecontaining glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). At least 14 mammalian galectins family members, which share structural similarities in their carbohydrate recognition domains (CRD), have been identified to date. Unlike the selectin family of proteins, the carbohydrate binding specificity of galectins is calcium-independent. A common function of galectins is to cross-link structures containing N-acetyl-lactosamine located at the cell surface and within the extracellular matrix. They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide, galectins can also be secreted by one or more unidentified, non-classical, secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins have been classified into the prototype galectins(1, 2, 5, 7, 10, 11, 13, 14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins(Galectin3) containing one CRD linked to a nonlectin domain, and the tandemrepeat Galectins(4, 6, 8, 9, 12) consisting of two CRDs joined by a linker peptide.Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.

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Human Interleukin 1 Family Member 10 (IL-1F10) is thought to participate in a network of Interleukin 1 cytokine family members to regulate adapted and innate immune responses. IL-1F10 was expressed in fetal skin, spleen and tonsil, mostly in the basal epithelia of skin and in proliferating B-cells of the tonsil. IL-1F10 binds soluble IL-1 receptor type 1 and may be implicated in regulating adapted and innate immune responses. Two alternatively spliced transcript variants encoding the same protein have been reported.

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Interleukin-1 alpha (IL1 alpha) is a cytokine member of the interleukin-1 family. IL-1 consists of two distinct forms: IL1 alpha and IL1 beta that recognize the same cell surface receptors but are distinct proteins with approximately 25% amino acid sequence identity. IL1 alpha is constitutively produced by epithelial cells and plays an essential role in maintenance of skin barrier function. Upon stimulation, a wide variety of cells including osteoblasts, monocytes, macrophages can be induced to express IL1 alpha. IL1 alpha possesses a wide range of metabolic, physiological, haematopoietic activities, and is critically involved in the regulation of the immune responses and inflammatory responses.

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Retinol Binding Protein 4 (RBP4) is a member of the Lipocalin family and in the blood. RBP4 is the specific vector for retinol. RBP4 is expressed and secreted by adipose tissue, and is associated with insulin resistance. RBP4 delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin to prevents its loss by filtration through the kidney glomeruli. Defects in RBP4 cause retinol-binding protein deficiency and can cause night vision problems.

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Tumor Necrosis Factor beta (TNF- beta ) is a secreted protein belonging to the tumor necrosis factor family. TNF- beta binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM in homotrimeric form, binds to TNFRSF3/LTBR in heterotrimeric form with LTB. TNF- beta forms heterotrimers with lymphotoxin-beta, which anchors TNF- beta to the cell surface. TNF- beta mediates the inflammatory, immunostimulatory, and antiviral response, involves in the formation of second lymphoid organs during development, has a role in apoptosis. TNF- beta is produced by lymphocytes and cytotoxic for a variety of tumor cells in vitro and in vivo.

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Interleukin-20 (IL-20) is a member of the IL-10 family of regulatory cytokines that includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences but they are dissimilar in their biological functions. IL-20 exhibits approximately 28% amino acid identity with IL-10 and 76% amino acid identity with mouse IL-20. There are two heterodimeric receptor complexes for IL-20. The first is composed of IL-20 R alpha and IL-20 R beta . The second is composed of IL-22 R and IL-20 R beta . Whereas the IL-22 R/IL-20 R beta complex is shared with IL-24, the IL-20 R alpha/IL-20 R beta complex is shared with both IL-19 and IL-24. IL-20 has been shown to initiate transduction cascades involving STAT3 and stimulates the induction of pro-inflammatory genes including TNF- alpha and MCP-1. Initial functional studies using transgenic mice suggest that IL-20 has the ability to regulate skin development. The over-expression of both human and mouse forms of IL-20 results in keratinocyte hyper-proliferation, abnormal epidermal differentiation, and neonatal lethality. In humans, IL-20 and its receptors are up-regulated in psoriatic skin, and polymorphisms in the IL-20 gene have been associated with plaque-type psoriasis. IL-20 may also have a role in hematopoiesis. It enhances the proliferation of multi-potential progenitors in vitro and increases their numbers and cell cycling status in IL-20 transgenic mice. IL-20 is also shown to suppress COX-2 and PGE2 and acts as an inhibitor of angiogenesis in model systems.

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Protein-Tyrosine Phosphatase 1C (PTP1C) belongs to the protein-tyrosine phosphatase family.which is known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP1C is highly expressed in leukocyte cell type. It contains two SH2 domains and one tyrosine-protein phosphatase domain. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. In addition, PTP1C also modulates signaling by tyrosine phosphorylated cell surface receptors.

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Human N-Glycosylase/DNA Lyase is a DNA repair enzyme, which incises DNA at 8-oxoG residues, and excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damage DNA

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Stratifin (SFN) belongs to the 14-3-3 family of proteins that act as important regulators of intracelluar signal transduction through their ability to bind specific motifs phosphorylated on serine or threonine. There are at least seven isoforms that have been identified in mammals (beta, gamma, epsilon, sigma, zeta, tau and eta). SFN can detected in many tissues, highly expressed in stratified squamous keratinizing epithelium. SFN is indicated as an epithelial cell marker and serves as a tumor suppressor whose expression can be down regulated by methylation. In addition, SFN plays a key role in maintaining the G2 checkpoint in cells and preventing mitotic death.

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Sentrin-Specific Protease 7 (SENP7) acts as a SUMO-2/3-specific protease

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Uteroglobin-Related Protein 1 (UGRP1) belongs to the secretoglobin family which has been suggested to play a role in lung inflammation and allergic diseases. UGRP1 is a 17 kDa secreted homodimeric protein that shows amino acid sequence similarity with uteroglobin. UGRP1 is expressed predominantly in the lung and low levels of expression are detected in the thyroid. Expression of UGRP1 in lung epithelial cells is enhanced by IL-10 and decreased through the activities of IL-9 and IL-5. UGRP1 interacts with the macrophage scavenger receptor with collagenous structure which is expressed by alveolar macrophages in the lung. It have suggested that UGRP1 may be involved in inflammation and pathogen clearance in the lung by binding to its receptor.

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Heat Shock Protein beta -11 (HSPB11) is a stress-responsive protein that is required to deal with proteotoxic stresses. HSPB11 is composed of an IFT complex B composed of IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11 and IFT20 and is detected in placenta. HSPB11 has beeb shown to form oligomeric complexes and prevent the aggregation of in vitro denaturated aldolase and glyceraldehyde-3-phosphate dehydrogenase in accordance with the chaperone model of HSPB1 and HSPB5. HSPB11 overexpression protected against etoposide-induced cell death that correlated with a decreased release of mitochondrial Cytochrome C into the cytosol. Inhibition of HSP90 function completely abrogated the protective effect of HSPB11. This data suggests that at least in the case of HSPB11, interaction with other chaperone machines besides HSPA1A may contribute to functional specificity and cellular functioning.

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Peptidyl-Prolyl Cis-Trans Isomerase-Like 1 (PPIase) belongs to the cyclophilin-type PPIase family

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Galactose Mutarotase (GALM) is a cytoplasmic enzyme that belongs to the Aldose Epimerase family

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There exists two types of tryptophanyl tRNA synthetases, the cytoplasmic form called WARS, the mitochondrial form called WARS2. WARS catalyzes the aminoacylation of tRNA (trp) with tryptophan and is induced by interferon. WARS regulates ERK, Akt, eNOS activation pathway, which are related with angiogenesis, cytoskelatal reorganization and shear stess-reponsive gene expression.

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CST7 is a secreted protein and primarily expressed in peripheral blood cells and spleen.It is belongs to the cystatin family. The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions. This gene encodes a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system.

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ICAM-2 is a 55-65 kD transmembrane glycoprotein possessing 2 extracellular Ig domains, a single transmembrane domain, and a short 26-amino acid cytoplasmic domain. ICAM-2 is expressed on most leukocytes, and is strongly expressed on vascular endothelial cells. Interactions of ICAM-2 and the integrin receptors mediate cell adhesion in a wide range of lymphocyte, monocyte, natural killer cell, and granulocytewith other cells, and play important roles in many adhesion-dependent immune and inflammation responses, such as T cell aggregation, NK-cell cytotoxicity and migration, lymphocyte recirculation, etc. Serum levels of ICAM-2 correlated significantly with the inflammatory and course sequences of trichinosis in mice and had a similar relation with blood eosinophilia. So, estimation of ICAM-2 serum levels may prove useful in diagnosis of trichinosis recent infections, and in monitoring the prognosis and response to treatment.

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CD274, also known as B7-H1 or programmed death ligand 1 (PD-L1), is a 40 kD type I transmembrane protein and a member of the B7 family within the immunoglobulin receptor superfamily. Programmed death-1 ligand-1 (PD-L1, CD274, B7-H1) has been identified as the ligand for the immunoinhibitory receptor programmed death-1(PD1/PDCD1) and has been demonstrated to play a role in the regulation of immune responses and peripheral tolerance. By binding to PD1 on activated T-cells and B-cells, PD-L1 may inhibit ongoing T-cell responses by inducing apoptosis and arresting cell-cycle progression. Accordingly, it leads to growth of immunogenic tumor growth by increasing apoptosis of antigen specific T cells and may contribute to immune evasion by cancers. PD-L1 thus is regarded as promising therapeutic target for human autoimmune disease and malignant cancers.

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The Interferon- alpha/ beta Receptor 1 (IFN- alpha/ beta R1) is a receptor which binds Type I Interferons including Interferon- alpha and - beta . It is a cell surface receptor and heteromeric receptor composed of one chain with two subunits referred to as IFNAR1 and IFNAR2. IFN- alpha/ beta R1, in association with IFN- alpha/ beta R2, is required for propagating antiviral signal transduction triggered by IFN- alpha and IFN- beta . IFN- alpha/ beta R1 interacts very weakly or not at all with type 1 interferons and does not stably interact with IFN- alpha/ beta R2. Ligands associate with IFN- alpha/ beta R2, and this complex subsequently forms a stable ternary assembly with IFN- alpha/ beta R1. IFN- alpha/ beta R1 also associates with IFN- gamma R2 even in the absence of IFN- gamma stimulation. Human IFN- alpha/ beta R1 contains a nuclear localization signal in its extracellular domain that is required for receptor translocation to the nucleus following interaction with ligand. Interferon stimulation results in an immunologic response that is especially associated with viruses.

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Complement Factor B (CFB) belongs to the peptidase S1 family of enzymes. It is expressed by hepatocytes and macrophages and localizes to the major histocompatibility complex (MHC) class III region on chromosome 6. CFB which is a component of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb. The active subunit Bb is a serine protease which associates with C3b to form the alternative pathway C3 convertase. Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

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Chitotriosidase-1 (CHIT1) is a glycoprotein that belongs to the Glycosyl Hydrolase 18 family and Chitinase class II subfamily

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Nectin-1 is a type I transmembrane glycoprotein belonging to the Ig superfamily. Nectin-1 promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between Nectin-1 and Nectin-3 and between Nectin-1 and Nectin-4. Nectin ECDs contain three Ig like domains: an N terminal V type that mediates ligand binding, and two C2 type. Nectin-1 binds viral Glycoprotein D to mediate Herpesvirus (but not Poxvirus) entry into vaginal mucosa, sensory neurons and fibroblasts. In forming adherens junctions and synapses, Nectin-1 and Nectin-3 initiate cell-cell interactions, recruiting alphav beta 3 integrin extracellularly and cadherins intracellularly through afadin and other junctional proteins. These interactions organize the cytoskeleton, strengthen attachment to basement membrane and promote further cell-cell connections. Nectin-1 and Nectin-3 have been found to localize assymetrically along the chemical synapse, with Nectin-1 primarily on the axonal side and Nectin-3 on the dendritic side. Deficiency of Nectin-1 can result in cleft lip/palate ectodermal dysplasia. Nectin-1 downregulation in epithelial cancers is mediated in part by ectodomain shedding, but it may contribute to invasiveness.

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Oncostatin-M-Specific Receptor Subunit beta (OSMR beta ) is a 150 - 180 kDa member of the IL-6 receptor family. OSMR beta associates with gp130 to form the type II OSM receptor, the receptor is responsive to OSM. Gp130 subunit is shared by other IL-6 family cytokine receptors, and OSMR beta associates with gp130-like receptor (GPL) to form a receptor complex responsive to IL-31. The human OSMR beta cDNA encodes a 979 amino acid (aa) precursor, the precursor includes a 27 aa signal sequence, a 712 aa extracellular domain (ECD), a 22 aatransmembrane segment, and a 218 aa cytoplasmic domain. The ECD contains one partial and one complete hematopoietin domain, an Ig-like domain, and three Fibronectin type-III domains.

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Osteoactivin is an intracellular glycoprotein belongs to the NMB/pMEL-17 family, which is asscociated with cell endosomal/lysomal compartments. Human Osteoactivin is a 560 amino acid type I transmembrane protein, and one alternate splice form shows a 12 amino acid insert between amino acid 339-340. An additional 206 amino acid isoform shows a mutation at position 181 that results in a 26 amino acid substitution for the C-terminal 380 amino acids. Cells knowns to express Osteoactivin include fibroblast, osteoblasts, myeloid dendritic cell, melanocytes, plus fetal chondrocytes and stratum basale keratinocytes, macrophages/keratinocytes.

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Semaphorin-5A (SEMA5A) is a member of the Semaphorin family of axon guidance molecules. SEMA5A is a 140 kDa protein. Class 5 Semaphorins are type I transmembrane glycoproteins with an N- terminal Sema domain and multiple juxtamembrane type 1 Thrombospondin (TSP) repeats within their extracellular domains. SEMA5A is expressed in neuroepithelial cells surrounding retinal axons, oligodendrocytes, the base of limb buds, the mesoderm surrounding cranial vessels , and the cardiac atrial septum and endocardial cushions, Human SEMA5A cDNA encodes a signal sequence, a extracellular domain (ECD), a transmembrane sequence and an cytoplasmic portion. SEMA5A mutations have been implicated in the genetic syndrome,cri-du-chat,while some polymorphisms may increase risk for neurodegenerative diseases such as Parkinson. The expression of SEMA5A may be upregulated in metastatic cancer cells and downregulated in autism.

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beta -2-Microglobulin (B2M) is a secreted protein with 1 Ig-like C1-type (immunoglobulin-like) domain which belongs to the beta-2-microglobulin family. B2M component of major histocompatibility complex (MHC) class I molecules, involved in the presentation of peptide antigens to the immune system. Polymers of beta 2-microglobulin can be found in tissues from patients on long-term hemodialysis. B2M is a protein found on the surface of many cells and plentiful on the surface of white blood cells. Serum B2M concentration is increased in renal diseases, various malignant diseases and some inflammatory and autoimmune disorders. B2M may adopt the fibrillar configuration of amyloid in certain pathologic states. The capacity to assemble into amyloid fibrils is concentration dependent. B2M has been shown as a marker for monitoring inflammatory disease activity and it appears likely to have a destructive role in amyloidosis-related arthritis. B2M might be involved in the OA (osteoarthritis) pathogenesis. Defects in B2M are the cause of hypercatabolic hypoproteinemia. Affected individuals show marked reduction in serum concentrations of immunoglobulin and albumin, probably due to rapid degradation. B2M could be a potential therapeutic target in ovarian cancer.

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Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. They are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. Serpin E1 is a secreted protein which belongs to the Serpin family. Serpin E1 acts as 'bait' for tissue plasminogen activator, urokinase, and protein C. Its rapid interaction with TPA may function as a major control point in the regulation of fibrinolysis. Defects in SERPINE1 are characterized by abnormal bleeding due to Serpin E1 defect in the plasma. High concentrations of Serpin E1 have been associated with thrombophilia which is an autosomal dominant disorder in which affected individuals are prone to develop serious spontaneous thrombosis.