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The EGFR subfamily of receptor tyrosine kinases is composed of EGFR, ErbB2, ErbB3 and ErbB4. The EGFR shares 43% - 44% aa sequence identity with the ECD of human EGFR subfamily. All these family members are type I transmembrane glycoproteins with an extracellular ligand binding domain. The extracellular ligand binding domain is containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain. Ligand binding could induce EGFR homodimerization and heterodimerization with ErbB2, resulting in cell signaling, heterodimerization tyrosine phosphorylation and kinase activation. It can bind EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, epigen, and so on. Its signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR is overexpressed in different tumors. Several anti-cancer drugs use EGFR as target.

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Programmed cell death 1 ligand 1 (PD-L1) is also known as cluster of differentiation (CD274) or B7 homolog 1 (B7-H1), is a member of the growing B7 family of immune molecules and is involved in the regulation of cellular and humoral immune responses. B7-H1 is a cell surface immunoglobulin superfamily with two Ig-like domains within the extracellular region and a short cytoplasmic domain. PD-L1 is highly expressed in the heart, skeletal muscle, placenta and lung and weakly expressed in the thymus, spleen, kidney and liver. PD-L1 is expressed on activated T-cells, B-cells, dendritic cells, keratinocytes and monocytes. PD-L1 is up-regulated on T- and B-cells, dendritic cells, keratinocytes and monocytes after LPS and IFNG activation and up-regulated in B-cells activated by surface Ig cross-linking. PD-L1 involve in the costimulatory signal, essential for T-cell proliferation and production of IL10 and IFNG, in an IL2-dependent and a PDCD1-independent manner.

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Myostatin is a TGF-beta family member that acts as an inhibitor of skeletal muscle growth. This muscle-specific cytokine interacts with Activin type I and type II receptors, and suppresses myoblast proliferation by arresting cell-cycle in the G1 phase. Suppression of myostatin activity facilitates muscle formation, and may be useful in reducing and/or preventing adiposity and type-2 diabetes. Myostatin activity can be blocked by the activin-binding protein follistatin, and by the propeptide of myostatin. Recombinant Human/Murine/Rat Myostatin is a 25.0 kDa protein consisting of two identical 109 amino acid polypeptides linked by a single disulfide bond. The amino acid sequence of mature myostatin is extremely conserved across species, and is the same in murine, rat, chicken, turkey, porcine, and human. Myostatin is expressed as the C-terminal part of a precursor polypeptide, which also contains a short N-terminal signal sequence for secretion, and a propeptide of 243 amino acids. After dimerization of this precursor, the covalent bonds between the propeptide and the mature ligand are cleaved by furin-type proteases. However, the resulting two proteins remain associated through non-covalent interactions, and are secreted as a latent complex.

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Visfatin is a 55 kDa protein produced and secreted primarily by white adipose tissue. Recently, Visfatin was isolated from visceral fat deposits and shown to possess insulin-mimetic activity. Like insulin, Visfatin exerts hypoglycemic effects by interacting with the insulin receptor. The binding affinity of Visfatin for the insulin receptor is similar to that of insulin, but it does not compete with insulin, suggesting that the two proteins interact with different receptor sites. The circulating levels of Visfatin are much lower than those of insulin and are not affected by feeding, implying that the hypoglycemic effect of Visfatin may not be of physiological importance. The plasma Visfatin levels, like those of Leptin, correlate positively with the percent of body fat and increase during the development of obesity. Another similarity between Visfatin and Leptin is that their amino acid sequence is highly conserved across different mammalian species and shows no homology to any known protein. Receptors for both Leptin (Ob-R) and Visfatin (i.e. the insulin receptor) are expressed by neurons within the arcuate nucleus of the hypothalamus, a brain area that plays a pivotal role in the regulation of energy metabolism. Although the metabolic function of Visfatin is still unknown, it appears that this newly identified adipocytokine might play an important role, similar to that of Leptin, in the regulation of body weight, i.e. as an afferent signal reflecting excess body fat. Recombinant human Visfatin is a 52.5 kDa protein containing 465 amino acid residues (isoform 1).

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Programmed Death-1 (PD-1), firstly cloned from mouse T cell hybridoma 2B4.11, is one member of CD28/CTLA-4 superfamily. PD-1 belongs to type I transmembrane protein and acts as an important immunosuppressive molecule. The cytoplamsic tail of PD-1 contains two structural motifs, an immunoreceptor tyrosine-based inhibitory motif (ITIM) and an immunoreceptor tyrosine-based switch motif (ITSM) formed by two tyrosine residues which make the difference in PD-1 signal mediating. Mouse PD-1 is expressed in thymus and shares about 69% aa sequence identity with human PD-1. Recently, programmed death-1 (PD-1) with its ligands, programmed death ligand B7H1 (PD-L1) and B7DC (PD-L2), was found to regulate T-cell activation and tolerance, upon ligand binding, inhibiting T-cell effector functions in an antigen-specific manner. PD-1 gene knocked out mice would induce some autoimmune diseases, which suggests that PD-1 acts as a co-inhibitory molecule actively participating in maintaining peripheral tolerance. Thus, PD-1 may be a useful target for the immunologic therapy of carcinoma,infection,autoimmune diseases as well as organ transplantation.

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T cell immunoglobulin and mucin domain-3 (TIM3), also called hepatitis A virus cellular receptor 2 (HAVCR2), is a transmembrane glycoprotein of the TIM family of immune regulating molecules and plays an important role in the Th1-mediated immune response. TIM3 is expressed on the Th1 cells, CD8 T-cells, monocytes, and dendritic cells, but not on Th2 cells. TIM3 expressed by monocytes and dendritic cells facilitates phagocytosis of apoptotic cells and up-regulates cross-presentation of apoptotic cell-associated antigens through interaction with phosphatidylserine. Engagement of TIM3 by its ligand galectin-9 induces a range of immunosuppressive functions which enhance immune tolerance and inhibit anti-tumor immunity. Stimulation of TIM3 with an agonistic antibody promotes inflammation through the activation of innate immune cells. TIM3 is also regarded as a potential target molecule for immunotherapy. TIM3 and programmed cell death 1 (PD-1) as two important coinhibitory regulators of T cell responses, have been implicated with the T-cell dysfunction or exhaustion associated with chronic HBV infection including HBV-related HCC.

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Interleukin-22(IL-22) is a member of a group of the IL-10 family, a class of potent mediators of cellular inflammatory responses. IL-22 is produced by activated DC and T cells. IL-22 and IL-10 receptor chains play a role in cellular targeting and signal transduction. It can initiate and regulate innate immune responses against bacterial pathogens especially in epithelial cells such as respiratory and gut epithelial cells. IL-22 along with IL-17 likely plays a role in the coordinated response of both adaptive and innate immune systems. IL-22 also promotes hepatocyte survival in the liver and epithelial cells in the lung and gut similar to IL-10. Biological activity of IL-22 is initiated by binding to a cell-surface complex consisting of IL-22R1 and IL-10R2 receptor chains. IL-22 biological activity is further regulated by interactions with a soluble binding protein, IL-22BP. IL-22BP and an extracellular region of IL-22R1 share sequence similarity. In some cases, the pro-inflammatory versus tissue-protective functions of IL-22 are regulated by cytokine IL-17A.

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Interleukin-12 (IL-12), also known as Natural Killer Cell Stimulatory Factor (NKSF) or Cytotoxic Lymphocyte Maturation Factor (CLMF), is a heterodimeric pleiotropic cytokine made up of a 40 kDa (p40) subunit and a 35 kDa (p35) subunit. IL-12 is produced by macrophages and B lymphocytes and has been shown to have multiple effects on T cells and Natural Killer (NK) cells. Some of these IL-12 activities include the induction of IFN-gamma and TNF in resting and activated T and NK cells; the enhancement of cytotoxic activity of resting NK and T cells, the stimulation of resting T cell proliferation in the presence of a comitogen; and the enhancement of NK cell proliferation. Current evidence indicates that IL-12 is a key mediator of cellular immunity and induces the differentiation of Th1 cells from precursor T helper cells. Based on its activities, it has been suggested that IL-12 may have therapeutic potential as a vaccine adjuvant that promotes cellular immunity and as an antitumor and anti viral agent.

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Calcitonin is a secreted protein which belongs to the calcitonin family. Calcitonin is cleaved into the following two chains: Calcitonin and Katacalcin. Katacalcin is a potent plasma calcium-lowering peptide. Calcitonin is a 32-amino acid linear polypeptide hormone. Calcitonin acts to reduce blood calcium (Ca2+), opposing the effects of parathyroid hormone (PTH). Its importance in humans has not been as well established as its importance in other animals, as its function is usually not significant in the regulation of normal calcium homeostasis. Calcitonin causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones.

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R-spondin-1 is also known as Roof plate-specific Spondin 1 (RSPO1) and cysteinerich and single thrombospondin domain containing protein 3 (Cristin 3), is a secreted protein which belongs to the R-Spondin family and encodes a secreted activator protein with two cystein-rich, furin-like domains and one thrombospondin type 1 domain. All Rspondins regulate Wnt/?-catenin signaling, but have distinct expression patterns. Like other R-Spondins, R-Spondin-1 contains two adjacent cysteinerich furinlike domains (aa 34-135) with one potential N-glycosylation site, followed by a thrombospondin (TSP1) motif (aa 147-207) and a region rich in basic residues (aa 211-263). Only the furinlike domains are needed for ?-catenin stabilization. A putative nuclear localization signal at the C-terminus may allow some expression in the nucleus. Potential isoforms of 200 and 236 aa have an alternate, shorter N-terminus or are missing aa 146-208, respectively. R-Spondin-1 is expressed in early development at the roof plate boundary and is thought to contribute to dorsal neural tube development. Human RSPO1 disruption results in a recessive syndrome characterized by XX sex reversal, palmoplantar hyperkeratosis and predisposition to squamous cell carcinoma of the skin. It has been shown that the complete female-to-male sex reversal is due to the absence of the testis-determining gene, SRY. R-Spondin-1 regulates Wnt/?-catenin by competing with the Wnt antagonist DKK1 for binding to the Wnt co receptors, Kremen and LRP6, reducing their DKK1 mediated internalization. Reports differ on whether R-spondin 1 binds LRP6 directly.

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Renin is also known as REN and angiotensinogenase, is a circulating enzyme that participates in the body's renin-angiotensin system (RAS), and plays an essential role in the elevation of arterial blood pressure and increased sodium retention by the kidney. Renin activates the renin-angiotensin system by cleaving angiotensinogen, produced by the liver, to yield angiotensin I, which is further converted into angiotensin II by ACE, the angiotensin-converting enzyme primarily within the capillaries of the lungs. Renin is secreted from kidney cells, which are activated via signaling from the macula densa, which responds to the rate of fluid flow through the distal tubule, by decreases in renal perfusion pressure (through stretch receptors in the vascular wall), and by sympathetic nervous stimulation, mainly through beta-1 receptor activation. Renin can bind to ATP6AP2, which results in a fourfold increase in the conversion of angiotensinogen to angiotensin I over that shown by soluble renin. In addition, renin binding results in phosphorylation of serine and tyrosine residues of ATP6AP2. The level of renin mRNA appears to be modulated by the binding of HADHB, HuR and CP1 to a regulatory region in the 3' UTR. An over-active renin-angiotension system leads to vasoconstriction and retention of sodium and water. These effects lead to hypertension. Therefore, renin inhibitors can be used for the treatment of hypertension.

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PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs, PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet alpha-granules, and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is a high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB. Recombinant Human PDGF-BB is a 24.3 kDa disulfide-linked homodimer of two beta chains (218 total amino acids).

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Mouse Cxcl12 is a secreted and highly conserved protein which belongs to the intercrine alpha (chemokine CxC) family.CXCL12 is widely expressed in various organs including brain, kidney, skeletal muscle, heart, liver, and lymphoid organs. Cxcl12 activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. It also binds to atypical chemokine receptor ACKR3 which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. Cxcl12 has several critical functions during embryonic development such as B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. Cxcl12 plays an important role in acting as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. It stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. It also plays a protective role after myocardial infarction, induces down-regulation and internalization of ACKR3 expressed in various cells and stimulates the proliferation of bone marrow-derived b progenitor cells in the presence of IL-7 as well as growth of the stromal cell-dependent B-cell clone DW34 cells.

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Irisin is a proteolytic hormone released into circulation by skeletal muscle tissue during acute exercise, and is a derivative of the cleaved plasma membrane protein Fibronectin type III domain-containing protein 5 (FNDC5). Found in muscle tissue, FNDC5 is synthesized at increased levels during exercise as a result of the overexpression of the exercise-responsive transcriptional co-activator PGC-1alpha (peroxisome proliferator-activated receptor-gamma co-activator-1alpha). Like its parent polypeptide, Irisin can induce the browning of subcutaneous adipocytes, or the conversion of white adipose tissue (WAT or white fat) into brown (or beige) adipose tissue (BAT or brown fat). Given that brown fat can undergo thermogenesis, or the physiologic process of heat production, Irisin contributes to the metabolic process by increasing thermogenic function and glucose homeostasis. Irisin, thus, represents a link between exercise and "burning" of fats and/or sugars, and consequently may have relevance in the development of new treatments for diabetes and obesity. CHO cell-derived Recombinant Human/Murine/Rat Irisin is a glycosylated homodimer of 224 amino acid residues, whose monomer consists of 112 amino acid residues corresponding to the active portion of the 121-amino-acid length Irisin extracellular domain. Recombinant Human/Murine/Rat Irisin, appears to form a non-disulfide linked oligomeric structure in solution, has a calculated theoretical molecular weight of 25.2 kDa, but migrates at an apparent molecular weight of 28 kDa by SDS-PAGE analysis under reducing conditions due to glycosylation.

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Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The alpha-defensins are distinguished from the beta-defensins by the pairing of their three disulfide bonds. To date, six human beta-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. beta-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Murine BD-3 is a 4.6 kDa protein containing 41 amino acid residues.

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Tumor Necrosis Factor- alpha (TNF- alpha) is secreted by macrophages, monocytes, neutrophils, T-cells, and NK-cells following stimulation by bacterial LPS. Cells expressing CD4 secrete TNF- alpha while cells that express CD8 secrete little or no TNF- alpha. Synthesis of TNF- alpha can be induced by many different stimuli including interferons, IL2, and GM-CSF. The clinical use of the potent anti-tumor activity of TNF- alpha has been limited by the proinflammatory side effects such as fever, dose-limiting hypotension, hepatotoxicity, intravascular thrombosis, and hemorrhage. Designing clinically applicable TNF- alpha mutants with low systemic toxicity has been of intense pharmacological interest. Human TNF- alpha that binds to murine TNF-R55 but not murine TNF-R7, exhibits retained anti-tumor activity and reduced systemic toxicity in mice compared with murine TNF- alpha, which binds to both murine TNF receptors. Based on these results, many TNF- alpha mutants that selectively bind to TNF-R55 have been designed. These mutants displayed cytotoxic activities on tumor cell lines in vitro and have exhibited lower systemic toxicity in vivo. Recombinant Human TNF- alpha High Active Mutant differs from the wild-type by amino acid subsitution of amino acids 1-7 with Arg8, Lys9, Arg10 and Phe157. This mutant form has been shown to have increased activity with less inflammatory side effects in vivo.

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Angiopoietin-1 (Ang-1) is a secreted ligand for Tie-2, a tyrosine-kinase receptor expressed primarily on vascular endothelial cells and early hematopoietic cells. Ang-1/ Tie-2 signaling promotes angiogenesis during the development, remodeling, and repair of the vascular system. Transgenic mice lacking expression of either Ang-1 or Tie-2 fail to develop a fully functional cardiovascular system and die before birth. Postnatally, the angiogenic activity of Ang-1/Tie-2 is required during normal tissue repair and remodeling of the female endometrium in the menstrual cycle. Ang-1/Tie-2 signaling appears to be regulated by Angiopoietin-2 (Ang-2), a natural antagonist for Tie-2 that exerts its effects through an internal autocrine loop mechanism. In addition to suppressing endothelial cell activation by inhibiting the expression of adhesion and inflammatory molecules, Ang-1 enhances endothelial cell survival and capillary morphogenesis, and lessens capillary permeability. As such, Ang-1 has a potential to become an effective therapeutic agent for treating various endothelium disorders, including several severe human pulmonary diseases. The efficacy of cell-based Ang-1 gene therapy for acute lung injury (ALI) has recently been studied in a rat model of ALI (1). The results of this study show that such therapy can markedly improve lung condition and suggest that Ang-1 therapy may represent a potential new strategy for the treatment and/or prevention of acute respiratory distress injury (ARDI), a significant cause of morbidity and mortality in critically ill patients. Recombinant human ANG-1, derived from HeLa cells, is a C-terminal histidine tagged glycoprotein which migrates with an apparent molecular mass of 60.0 - 70.0 kDa by SDS-PAGE under reducing conditions. Sequencing analysis shows N-terminal sequences starting with Ser-20 and with Asp-70 of the 498 amino acid precursor protein.

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BAFF is mainly produced by innate immune cells such as neutrophils, monocytes, macrophages, dendritic cells, follicular dendritic cells. T cells, activated B cells, some malignant B cells and also non-lymphoid cells like astrocytes, synoviocytes and epithelial cells can also produce BAFF. BAFF binds three distinct receptors (BAFF-R, TACI and BCMA) expressed predominantly on B cells, although activated T cells also express BAFF-R. BAFF is a master regulator of peripheral B cell survival, and together with IL-6, promotes Ig class-switching and plasma cell differentiation. Besides its major role in B cell biology, BAFF co-stimulates activated T cells. Deregulated expression of BAFF leads to autoimmune disorders in mice. In humans, elevated levels of soluble BAFF have been detected in the serum of patients with various autoimmune diseases such as Sjoegren syndrome, Rheumatoid arthritis (RA), Multiple sclerosis (MS) and Systemic Lupus Erythematosus (SLE). BAFF has also increased levels in some lymphoid cancers. Processed human BAFF can either remain as a trimer, which is usual for TNF family ligands or assemble into 60-mer composed of 20 trimers. Mouse BAFF 60-mer has been identified in the serum of BAFF transgenic mice. Oligomerization of BAFF 3-mer into 60-mer in human BAFF is prevented by mutation of His218, a residue critical for 3-mer-to-3-mer interactions, but not for receptor binding. Despite the predominant functional role of processed BAFF in vivo, membrane-bound BAFF might also play a role. Indeed, soluble BAFF (3-mer) can trigger BAFF-R but not TACI or BCMA, whereas oligomeric forms of BAFF (BAFF 60-mer), which mimic membrane-bound BAFF, activate all BAFF receptors.

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Proenkephalin-A is a secreted protein that belongs to the opioid neuropeptide precursor family. Proenkephalin-A is an endogenous opioid polypeptide hormone which, via proteolyic cleavage, produces the enkephalin peptides [Met]enkephalin, and to a lesser extent, [Leu]enkephalin. Met- and Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. Proenkephalin-A (114-133) and Proenkephalin-A (237-258) increase glutamate release in the striatum. Proenkephalin-A (114-133) decreases GABA concentration in the striatum.

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Programmed Death-1 (PD-1), firstly cloned from mouse T cell hybridoma 2B4.11, is one member of CD28/CTLA-4 superfamily. PD-1 belongs to type I transmembrane protein and acts as an important immunosuppressive molecule. This family also include members of CD28, CTLA-4 and ICOS.The mouse Programmed Death-1 protein, encoded by PD-1 gene, comprises four parts including a putative 20 aa signal peptide, a 149 aa extracellular region, a 21 aa transmembrane domain and a 98 aa cytoplasmic region. The cytoplamsic tail of PD-1 contains two structural motifs, an immunoreceptor tyrosine-based inhibitory motif (ITIM) and an immunoreceptor tyrosine-based switch motif (ITSM) formed by two tyrosine residues which make the difference in PD-1 signal mediating. Mouse PD-1 is expressed in thymus and shares about 69% aa sequence identity with human PD-1. Recently, programmed death-1 (PD-1) with its ligands, programmed death ligand B7H1 (PD-L1) and B7DC (PD-L2), was found to regulate T-cell activation and tolerance, upon ligand binding, inhibiting T-cell effector functions in an antigen-specific manner. PD-1 gene knocked out mice would induce some autoimmune diseases, which suggests that PD-1 acts as a co-inhibitory molecule actively participating in maintaining peripheral tolerance. Thus, PD-1 may be a useful target for the immunologic therapy of carcinoma,infection,autoimmune diseases as well as organ transplantation.

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Sox2, also known as sex determining region Y (SRY)-box 2, belongs to a diverse family of structurally-related transcription factors whose primary structure contains a 79-residue DNA-binding domain, called high mobility group (HMG) box. It plays an essential role in maintaining the pluripotency of embryonic stem cells (ESC) and determination of cell fate. Microarray analysis showed that Sox2 regulates the expression of multiple genes involved in embryonic development including FGF-4, YES1 and ZFP206. Sox2 acts as a transcriptional activator after forming a ternary complex with Oct3/4 and a conserved non-coding DNA sequence (CNS1) located approximately 2 kb upstream of the RAX promoter. The introduction of Sox2, Oct4, Myc, and Klf4, into human dermal fibroblasts isolated from a skin biopsy of a healthy research fellow was sufficient to confer a pluripotent state upon the fibroblast genome. The reprogrammed cells thus obtained resemble ESC in morphology, gene expression, and in the capacity to form teratomas in immune-deficient mice. Sox2 and other transcription factors have been introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors and other nuclear proteins into primary as well as transformed cells. Recombinant human Sox2-TAT expressed in E. coli is a 36 kDa protein containing 330 amino-acid residues, including the 317 residues of full-length Sox2 and a 13-residue C-terminal TAT peptide (GGYGRKKRRQRRR).

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SPARC/Osteonectin is a secreted, evolutionarily conserved collagen-binding glycoprotein that is involved in a variety of cellular activities. It is highly expressed in tissues undergoing morphogenesis, remodeling and wound repair. SPARC/Osteonectin and its related peptides bind to numerous proteins of the extracellular matrix (ECM), affect ECM protein expression, influence cellular adhesion and migration, and modulate growth factor-induced cell proliferation and angiogenesis. SPARC/Osteonectin consists of three domains; an N-terminal acidic region that binds calcium ions with low affinity, a module containing two EF-hand motifs that bind calcium with high affinity, and a cysteine-rich follistatin-like domain. Recombinant human SPARC/Osteonectin is a glycoprotein containing 286 amino acids that migrates at an apparent MW of 43.7 kDa by SDS-PAGE analysis due to the effect of glycosylation.

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TIE-1 (Tyrosine Kinase with Ig and EGF Homology domains 1) and TIE-2/Tek comprise a receptor tyrosine kinase (RTK) subfamily. These receptors are expressed on endothelial and hematopoietic progenitor cells and play critical roles in angiogenesis, vasculogenesis and hematopoiesis. Human TIE-1 cDNA encodes a 1124 amino acid (aa) residue precursor protein with an 18aa signal peptide, a 727 aa extracellular domain and a 354 aa cytoplasmic domain. so far, two ligands have been described for TIE-2 [angiopoietin-1 (Ang1) and angiopoietin-2 (Ang2)], but no ligand was found for TIE-1.

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Mouse Chordin-Like 2, also known as CHL2, is a novel chordin family member with structural homology to CHL1 which is implicated in tumor angiogenesis. The mouse CHL2 gene encodes a 426 amino acids (aa) protein with a 25 aa signal peptide. The mature chain of CHL2 protein contains two potential N-linked glycosylation sites, one putative NLS and three 63 aa cysteine-rich von Willebrand type C repeats (CRs). CHL2 gene is weakly expressed in the liver and kidney, partly expressed in the connective tissues of reproductive organs such as ligaments of the ovary and oviduct in females, and of testis, epididymis and certain male accessory sex glands in males. Recombinant mCHL2 protein interacted directly with five BMPs and one GDF thereby inhibiting, in vitro, several BMP/GDF-dependent processes including, osteogenic differentiation of C2C12 mesenchymal progenitor cells by several BMPs, ATDC5 embryonal carcinoma cells by GDF5 and BMP4-dependent lymphohematopoietic (CD34+CD31hi and CD34+CD31lo) progenitor cell development from ES cells. CHL2 may inhibits BMPs activity by blocking their interaction with their receptors, and has a negative regulator effect on the cartilage formation/regeneration from immature mesenchymal cells, by preventing or reducing the rate of matrix accumulation. Also, it may play a role during myoblast and osteoblast differentiation, and maturation.

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GLIPR1L2 Peptide

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GRK6 Peptide

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GLIPR1L1 Peptide

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NOX4 Peptide

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DAF Peptide

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BATF3 Peptide