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T68306 | |||
INCB16562 is a novel, selective, and orally bioavailable small-molecule inhibitor of JAK1 and JAK2 markedly selective over JAK3. Treatment of myeloma cells with INCB16562 potently inhibited interleukin-6 (IL-6)-induced phosphorylation of STAT3. INCB16562 abrogated the protective effects of recombinant cytokines or bone marrow stromal cells and sensitized myeloma cells to cell death by exposure to dexamethasone, melphalan, or bortezomib. Oral administration of INCB16562 antagonized the growth of myeloma xenografts in mice and enhanced the antitumor activity of relevant agents in combination studies. INCB16562 is a potent JAK1/2 inhibitor and that mitigation of JAK/STAT signaling by targeting JAK1 and JAK2 will be beneficial in the treatment of myeloma patients, particularly in combination with other agents. ( source: Neoplasia. 2010 Jan;12(1):28-38. ). | |||
TN3364 | Apoptosis Dehydrogenase p38 MAPK ROS JAK | ||
Agrimonolide 是一种来自异香豆素的化合物,主要存在于草药Agrimonia pilosa Ledeb 中,具有显著的生物活性。Agrimonolide 通过抑制脂多糖(LPS)诱导的JAK-STATs 和p38 MAPKs 信号通路的激活而发挥抗炎作用。Agrimonolide 及其衍生物去甲阿戈莫内德已显示出能够有效提高肝细胞中胰岛素介导的糖原水平,可能在调节胰岛素抵抗的HepG2细胞中发挥关键作用。Agrimonolide 通过靶向卵巢癌细胞中的SCD1,对癌症的进展和诱导细胞死亡和凋亡表现出抑制作用。特别是,Agrimonolide 对A2780和SKOV-3细胞的增殖、迁移和侵袭表现出剂量依赖性的抑制,同时促进细胞凋亡。该化合物还被发现能诱导铁介导的细胞死亡,同时增加活性氧(ROS)和总铁的水平。Agrimonolide 很容易穿过血脑屏障,表明其在神经系统疾病的治疗应用方面具有潜力。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPH-02273 | JAK1 Protein, Human, Recombinant (His) | Human | Yeast | ||
Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor as well as interleukin (IL)-10 receptor. Directly phosphorylates STAT but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors.
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TMPH-02274 | JAK2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin.
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TMPH-02961 | JAK1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor as well as interleukin (IL)-10 receptor. Directly phosphorylates STAT but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors.
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TMPH-02272 | JAK1 Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway. Kinase partner for the interleukin (IL)-2 receptor as well as interleukin (IL)-10 receptor. Directly phosphorylates STAT but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors.
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TMPK-00474 | IL-22RA1 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
IL-22 receptor, also known as IL-22 R alpha 1 and CRF2-9, is an approximately 65 kDa transmembrane glycoprotein in the type II cytokine receptor family (CRF).Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation.
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TMPY-02647 | IFNAR1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interferon-alpha/beta receptor alpha chain (IFNAR1) is a type I membrane protein that forms one of the two chains of a receptor for interferons alpha and beta. Binding and activation of the receptor stimulate Janus protein kinases, which in turn phosphorylate several proteins, including STAT1 and STAT2. The encoded protein also functions as an antiviral factor. Tyk2 slows down IFNAR1 degradation and that this is due, at least in part, to inhibition of IFNAR1 endocytosis. Mutant versions of IFNAR1, in which Tyr466 is changed to phenylalanine, can act in a dominant-negative manner to inhibit phosphorylation of STAT2. These observations are consistent with a model in which IFNAR1 mediates the interaction between JAK kinases and the STAT transcription factors.
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TMPJ-00059 | IL-7 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Human Interleukin 7 (IL-7) is a potent lymphoid cell growth factor stimulating the proliferation of lymphoid progenitors. IL7 can associate with the hepatocyte growth factor (HGF) to form a hybrid cytokine that functions as a pre-pro-B cell growth-stimulating factor. Human IL7 cDNA encodes a 177 amino acid precursor protein containing a 25 amino acid signal peptide and a 152 amino acid mature protein. Human and mouse IL7 share 65% sequence identity in the mature region and both exhibit cross-species activity. IL-7 signals via IL-7 receptor (IL7R) activating multiple pathways including JaK/STAT and PI3K/AKT, which regulate lymphocyte survival, glucose uptake, proliferation, and differentiation. IL-7 is also associated with cytoplasmic IL2-R gamma for signal transduction.
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TMPY-04632 | IL-15 Protein, Human, Recombinant | Human | E. coli | ||
The protein encoded by the IL15 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 hematopoietic 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. Alternatively, spliced transcript variants of this gene have been reported.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03532 | LIF Protein, Human, Recombinant (His) | Human | HEK293 | ||
Leukemia inhibitory factor (LIF) is a pleiotropic glycoprotein belonging to the IL-6 family of cytokines. It is involved in growth promotion and cell differentiation of different types of target cells, influence bone metabolism, cachexia, neural development, embryogenesis, and inflammation. LIF has potent proinflammatory properties, being the inducer of the acute phase protein synthesis and affecting cell recruitment into the area of damage or inflammation. LIF is also one of the cytokines that are capable to regulate the differentiation of embryonic stem cells, hematopoietic, and neuronal cells. LIF binds to the specific LIF receptor (LIFR-α) which forms a heterodimer with a specific subunit common to all members of that family of receptors, the GP130 signal-transducing subunit. This leads to the activation of the JAK/STAT and MAPK cascades. Due to its polyfunctional activities, LIF is involved in the pathogenic events and development of many diseases of various origins.
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TMPY-04104 | LIF Protein, Human, Recombinant | Human | HEK293 | ||
Leukemia inhibitory factor (LIF) is a pleiotropic glycoprotein belonging to the IL-6 family of cytokines. It is involved in growth promotion and cell differentiation of different types of target cells, influence bone metabolism, cachexia, neural development, embryogenesis, and inflammation. LIF has potent proinflammatory properties, being the inducer of the acute phase protein synthesis and affecting cell recruitment into the area of damage or inflammation. LIF is also one of the cytokines that are capable to regulate the differentiation of embryonic stem cells, hematopoietic, and neuronal cells. LIF binds to the specific LIF receptor (LIFR-α) which forms a heterodimer with a specific subunit common to all members of that family of receptors, the GP130 signal-transducing subunit. This leads to the activation of the JAK/STAT and MAPK cascades. Due to its polyfunctional activities, LIF is involved in the pathogenic events and development of many diseases of various origins.
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TMPY-04278 | LIF Protein, Mouse, Recombinant | Mouse | HEK293 | ||
Leukemia inhibitory factor (LIF) is a pleiotropic glycoprotein belonging to the IL-6 family of cytokines. It is involved in growth promotion and cell differentiation of different types of target cells, influence bone metabolism, cachexia, neural development, embryogenesis, and inflammation. LIF has potent proinflammatory properties, being the inducer of the acute phase protein synthesis and affecting cell recruitment into the area of damage or inflammation. LIF is also one of the cytokines that are capable to regulate the differentiation of embryonic stem cells, hematopoietic, and neuronal cells. LIF binds to the specific LIF receptor (LIFR-α) which forms a heterodimer with a specific subunit common to all members of that family of receptors, the GP130 signal-transducing subunit. This leads to the activation of the JAK/STAT and MAPK cascades. Due to its polyfunctional activities, LIF is involved in the pathogenic events and development of many diseases of various origins.
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TMPY-00136 | IL-29 Protein, Human, Recombinant | Human | HEK293 | ||
Interleukin-29 (IL-29), also known as cytokine Zcyto21, Interferon lambda-1, IFN-lambda-1, and IFNL1, is a secreted protein that belongs to the IL-28 / IL-29 family. IL-29 is a cytokine with immunomodulatory activity. IL-29 is highly similar in amino acid sequence to the IL-28. IL-28 and IL-29 are induced by a viral infection and showed antiviral activity. IL-28 and IL-29 interacted with a heterodimeric class II cytokine receptor that consisted of IL-10 receptor beta (IL-10Rbeta) and an orphan class II receptor chain, designated IL-28Ralpha. IL-29 plays an important role in host defenses against microbes and its gene is highly upregulated in cells infected with viruses. IL-29 may play a role in antiviral immunity. IL-29 up-regulates MHC class I antigen expression. It is a Ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IL28RA. The ligand/receptor complex seems to signal through the Jak-STAT pathway.
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TMPY-05274 | IL-23R Protein, Human, Recombinant (His) | Human | HEK293 | ||
IL23R, also known as the IL23 receptor, belongs to the type I cytokine receptor family, Type 2 subfamily. It contains 2 fibronectin type-III domains and is expressed by monocytes, Th1, Th0, NK, and dendritic cells. Isoform 1 is specifically expressed in NK cells. IL23R associates with IL12RB1 to form the interleukin-23 receptor. It binds IL23 and mediates T-cells, NK cells, and possibly certain macrophage/myeloid cell stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis. Genetic variations in IL23R are associated with inflammatory bowel disease type 17 (IBD17). IBD17 is a chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. Genetic variations in IL23R also can cause susceptibility to psoriasis type 7.
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TMPY-05242 | CRLF2/TSLPR Protein, Human, Recombinant (His) | Human | HEK293 | ||
Overexpression of cytokine receptor-like factor 2 (CRLF2) due to chromosomal rearrangement has been observed in acute lymphoblastic leukemia (ALL) and reported to contribute to oncogenesis and unfavorable outcome in ALL. The high CRLF2 expression works with the IKZF1 deletion to drive oncogenesis of ALL and has significance in an integrated prognostic model for adult high-risk ALL. Thymic stromal lymphopoietin (TSLP) stimulates in-vitro proliferation of human fetal B-cell precursors. However, its in-vivo role during normal human B lymphopoiesis is unknown. Genetic alterations that cause overexpression of its receptor component, cytokine receptor-like factor 2 (CRLF2), lead to high-risk B-cell acute lymphoblastic leukemia implicating this signaling pathway in leukemogenesis. CRLF2 over-expression is a poor prognostic marker identifying a subset of HR T-ALL patients that could benefit from alternative therapy, potentially targeting the CRLF2 pathway. Cytokine receptor-like factor 2 ( CRLF2 ) rearrangement is found in approximately 50% of pediatric Ph-like B-cell acute lymphoblastic leukemia (B-ALL), and around 50% of CRLF2 + cases harbor JAK mutations. Cytokine receptor-like factor 2(CRLF2) plays an important role in the development of normal B lymphocytes, which can mediate early B cell proliferation and survival.
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TMPY-01872 | IL-28B Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin-28B (IL-28B) also known as Interferon lambda-3 and IFN-lambda-3, belongs to the type III interferon family of cytokines and are highly similar to IL-29. IL-28B belongs to the newly described interferon lambda (IFNλ) family of cytokines. IL-28B is a cytokine with immunomodulatory activity. It functions in Up-regulating MHC class I antigen expression. IL-28B displays potent antiviral activity and antitumor activity. This cytokine serves as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IL28RA. The ligand/receptor complex seems to signal through the Jak-STAT pathway. IL-28B, like IL-12, is capable of robustly enhancing adaptive immunity. Moreover, we describe for the first time how IL-28B reduces regulatory T-cell populations during DNA vaccination, whereas IL-12 increases this cellular subset. We also show that IL-28B, unlike IL-12, can increase the percentage of splenic CD8+ T cells in vaccinated animals and that these cells are more granular and have higher antigen-specific cytolytic degranulation compared with cells taken from animals that received IL-12 as an adjuvant.
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TMPY-01053 | Prolactin Receptor Protein, Human, Recombinant (His) | Human | HEK293 | ||
Prolactin receptor (PRLR) is a single-pass transmembrane receptor belonging to the type I cytokine receptor superfamily, and contains two fibronectin type-III domains. All class 1 ligands activate their respective receptors by clustering mechanisms. Ligand binding results in the transmembrane PRLR dimerization, followed by phosphorylation and activation of the molecules involved in the signaling pathways, such as Jak-STAT, Ras/Raf/MAPK. The PRLR contains no intrinsic tyrosine kinase cytoplasmic domain but associates with a cytoplasmic tyrosine kinase, JAK2. PRLR mainly serves as the receptor for the pituitary hormone prolactin (PRL), a secreted hormone that affects reproduction and homeostasis in vertebrates. PRLR can be regulated by an interplay of two different mechanisms, PRL or ovarian steroid hormones independently or in combination in a tissue-specific manner. The role of the hormone prolactin (PRL) in the pathogenesis of breast cancer is mediated by its cognate receptor (PRLR). Ubiquitin-dependent degradation of the PRLR that negatively regulates PRL signaling is triggered by PRL-mediated phosphorylation of PRLR on Ser349 followed by the recruitment of the beta-transducin repeats-containing protein (beta-TrCP) ubiquitin-protein isopeptide ligase. which altered PRLR stability may directly influence the pathogenesis of breast cancer.
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TMPY-01701 | IL-12RB1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin 12 receptor, beta 1 is also known as IL-12 receptor beta component, IL-12R subunit beta-1, and CD212 antigen (CD212). IL12RB1(CD212) is a subunit of the interleukin 12 receptor. IL12RB1(CD212) is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily. This protein binds to interleukin 12 (IL12) with a low affinity and is thought to be a part of the IL12 receptor complex. IL12RB1(CD212) forms a disulfide-linked oligomer, which is required for its IL12 binding activity. The coexpression of IL12RB1 and IL12RB2 proteins was shown to lead to the formation of high-affinity IL12 binding sites and reconstitution of IL12 dependent signaling. The lack of expression of this gene was found to result in the immunodeficiency of patients with severe mycobacterial and Salmonella infections. IL12RB1(CD212) Functions as an interleukin receptor that binds interleukin-12 with low affinity and is involved in IL12 transduction. It is associated with IL12RB2 it forms a functional, high-affinity receptor for IL12. IL12RB1(CD212) associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade.
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TMPY-05748 | CD45 Protein, Human, Recombinant (aa 26-577, His) | Human | HEK293 | ||
The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. CD45 is found expression specifically in hemotopietic cells. CD45 consists of an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains. It serves as an essential regulator of T-cell and B-cell antigen receptor signaling through either direct interaction with components of the antigen receptor complexes or by activating various Src family kinases required for the antigen receptor signaling and it also can suppress JAK kinases.
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TMPY-05308 | CD45 Protein, Human, Recombinant (aa 1-529, His) | Human | HEK293 | ||
The cluster of differentiation (CD) system is commonly used as cell markers in Immunophenotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Protein tyrosine phosphatase, receptor type C (CD45), also known as PTPRC is a member of the protein tyrosine phosphatase (PTP) family which is known for its function to serve as signaling molecules and to regulate a variety of cellular processes such as cell proliferation, differentiation, mitotic cycle and oncogenic transformation. CD45 is found expression specifically in hemotopietic cells. CD45 consists of an extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains. It serves as an essential regulator of T-cell and B-cell antigen receptor signaling through either direct interaction with components of the antigen receptor complexes or by activating various Src family kinases required for the antigen receptor signaling and it also can suppress JAK kinases.
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TMPY-05480 | IL-21R Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Interleukin-21 receptor, also known as IL-21 receptor, IL-21R, Novel interleukin receptor, IL21R, and NILR, is a single-pass type I membrane protein that belongs to the type I cytokine receptor family and Type 4 subfamily. Interleukin-21 (IL-21) belongs to a family of cytokines that bind to a composite receptor consisting of a private receptor (IL-21R) and the common cytokine receptor gamma chain ( gamma(C) ). The IL-21R is discovered as a novel member of the class-I-cytokine-receptor family and is selectively expressed in lymphoid tissues. IL-21R shows strong sequence homologies to the interleukin-4 receptor alpha chain gene (IL-4RA). The WSXWS motif of IL-21R appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. The box 1 motif of IL-21R is required for JAK interaction and/or activation. The IL-21R is widely distributed on lymphohematopoietic cells and IL21 impacts some cell types, including CD8+ memory T cells, NK cells, and subsets of CD4 memory T cells. Increased IL21 production is characteristic of certain autoimmune diseases and is likely to contribute to autoantibody production as well as pathological features of autoimmune disease. The critical role of IL21 in promoting humoral immune responses makes it an important focus of potential therapeutic interventions in conditions characterized by the overproduction of pathogenic autoantibodies.
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TMPY-01934 | IL-21R Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin-21 receptor, also known as IL-21 receptor, IL-21R, Novel interleukin receptor, IL21R, and NILR, is a single-pass type I membrane protein that belongs to the type I cytokine receptor family and Type 4 subfamily. Interleukin-21 (IL-21) belongs to a family of cytokines that bind to a composite receptor consisting of a private receptor (IL-21R) and the common cytokine receptor gamma chain ( gamma(C) ). The IL-21R is discovered as a novel member of the class-I-cytokine-receptor family and is selectively expressed in lymphoid tissues. IL-21R shows strong sequence homologies to the interleukin-4 receptor alpha chain gene (IL-4RA). The WSXWS motif of IL-21R appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. The box 1 motif of IL-21R is required for JAK interaction and/or activation. The IL-21R is widely distributed on lymphohematopoietic cells and IL21 impacts some cell types, including CD8+ memory T cells, NK cells, and subsets of CD4 memory T cells. Increased IL21 production is characteristic of certain autoimmune diseases and is likely to contribute to autoantibody production as well as pathological features of autoimmune disease. The critical role of IL21 in promoting humoral immune responses makes it an important focus of potential therapeutic interventions in conditions characterized by the overproduction of pathogenic autoantibodies.
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TMPY-00418 | IL-21R Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Interleukin-21 receptor, also known as IL-21 receptor, IL-21R, Novel interleukin receptor, IL21R, and NILR, is a single-pass type I membrane protein that belongs to the type I cytokine receptor family and Type 4 subfamily. Interleukin-21 (IL-21) belongs to a family of cytokines that bind to a composite receptor consisting of a private receptor (IL-21R) and the common cytokine receptor gamma chain ( gamma(C) ). The IL-21R is discovered as a novel member of the class-I-cytokine-receptor family and is selectively expressed in lymphoid tissues. IL-21R shows strong sequence homologies to the interleukin-4 receptor alpha chain gene (IL-4RA). The WSXWS motif of IL-21R appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. The box 1 motif of IL-21R is required for JAK interaction and/or activation. The IL-21R is widely distributed on lymphohematopoietic cells and IL21 impacts some cell types, including CD8+ memory T cells, NK cells, and subsets of CD4 memory T cells. Increased IL21 production is characteristic of certain autoimmune diseases and is likely to contribute to autoantibody production as well as pathological features of autoimmune disease. The critical role of IL21 in promoting humoral immune responses makes it an important focus of potential therapeutic interventions in conditions characterized by the overproduction of pathogenic autoantibodies.
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TMPY-03547 | IL-10 Protein, Human, Recombinant | Human | E. coli | ||
IL-10 is an anti-inflammatory cytokine that belongs to the IL-10 family. It is produced by a variety of cell lines, including T-cells, macrophages, mast cells, and other cell types, while it is produced primarily by monocytes and to a lesser extent by lymphocytes. IL-10 is mainly expressed in monocytes and Type 2 T helper cells (TH2), mast cells, CD4+CD25+Foxp3+ regulatory T cells, and also in a certain subset of activated T cells and B cells. IL-10 has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL-10 can block NF-kappa B activity and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract. The importance of interleukin 10 for counteracting excessive immunity in the human body is revealed by the fact that patients with Crohn's disease react favorably towards treatment with bacteria producing recombinant IL-10. IL-10 inhibits the synthesis of some cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T-cells. It also displays a potent ability to suppress the antigen-presentation capacity of antigen-presenting cells. However, it is also stimulatory towards certain T cells and mast cells and stimulates B cell maturation and antibody production.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01845 | IL-10 Protein, Human, Recombinant (His) | Human | HEK293 | ||
IL-10 is an anti-inflammatory cytokine that belongs to the IL-10 family. It is produced by a variety of cell lines, including T-cells, macrophages, mast cells, and other cell types, while it is produced primarily by monocytes and to a lesser extent by lymphocytes. IL-10 is mainly expressed in monocytes and Type 2 T helper cells (TH2), mast cells, CD4+CD25+Foxp3+ regulatory T cells, and also in a certain subset of activated T cells and B cells. IL-10 has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL-10 can block NF-kappa B activity and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract. The importance of interleukin 10 for counteracting excessive immunity in the human body is revealed by the fact that patients with Crohn's disease react favorably towards treatment with bacteria producing recombinant IL-10. IL-10 inhibits the synthesis of some cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T-cells. It also displays a potent ability to suppress the antigen-presentation capacity of antigen-presenting cells. However, it is also stimulatory towards certain T cells and mast cells and stimulates B cell maturation and antibody production.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05064 | IL-10 Protein, Mouse, Recombinant | Mouse | E. coli | ||
IL-10 is an anti-inflammatory cytokine that belongs to the IL-10 family. It is produced by a variety of cell lines, including T-cells, macrophages, mast cells, and other cell types, while it is produced primarily by monocytes and to a lesser extent by lymphocytes. IL-10 is mainly expressed in monocytes and Type 2 T helper cells (TH2), mast cells, CD4+CD25+Foxp3+ regulatory T cells, and also in a certain subset of activated T cells and B cells. IL-10 has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. IL-10 can block NF-kappa B activity and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract. The importance of interleukin 10 for counteracting excessive immunity in the human body is revealed by the fact that patients with Crohn's disease react favorably towards treatment with bacteria producing recombinant IL-10. IL-10 inhibits the synthesis of some cytokines, including IFN-gamma, IL-2, IL-3, TNF, and GM-CSF produced by activated macrophages and by helper T-cells. It also displays a potent ability to suppress the antigen-presentation capacity of antigen-presenting cells. However, it is also stimulatory towards certain T cells and mast cells and stimulates B cell maturation and antibody production.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01410 | IL-3R alpha/CD123 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin-3 receptor subunit alpha, also known as IL-3 receptor subunit alpha, IL-3R-alpha, CD123, and IL3RA, is a single-pass type I membrane protein that belongs to the type I cytokine receptor family and Type 5 subfamily. The specific alpha subunit of the interleukin-3 receptor (IL-3Ralpha, CD123) is strongly expressed in various leukemic blasts and leukemic stem cells and seems to be an excellent target for the therapy of leukemias. The WSXWS motif of IL3RA appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. The box one motif of IL3RA is required for JAK interaction and/or activation. IL3RA represents a unique marker for primitive leukemic stem cells. Targeting of IL3RA may be a promising strategy for the preferential ablation of AML cells. Aberrant IL3RA expression is a good marker for monitoring of minimal residual disease. IL3RA is strongly expressed in various leukemic blasts and leukemic stem cells and seems to be an excellent target for the therapy of leukemias. Recent studies have shown that interleukin-3 receptor alpha (CD123) is highly expressed on leukemia stem cells of patients with acute myeloid leukemia, and is correlated with tumor load and poor prognosis. CD123 was highly expressed in the bone marrow of the patients with myelodysplastic syndrome (MDS), significantly correlated with the proportion of bone marrow blasts, and thus might be the marker of MDS malignant clone. IL3RA is also a useful new marker for distinguishing B-cell disorders with circulating villous lymphocytes as its expression is characteristic of typical hairy cell leukemia (HCL) with high sensitivity and specificity.
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TMPY-05644 | CD25/IL2R alpha Protein, Rhesus, Recombinant (His & Avi), Biotinylated | Rhesus | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05090 | CD25/IL2R alpha Protein, Rat, Recombinant (His) | Rat | Baculovirus-Insect Cells | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01923 | CD25/IL2R alpha Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05584 | CD25/IL2R alpha Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01103 | CD25/IL2R alpha Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03776 | CD25/IL2R alpha Protein, Cynomolgus, Recombinant | Cynomolgus | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03644 | CD25/IL2R alpha Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
CD25 (alpha-chain of the IL-2 receptor, or IL2RA), is a type I transmembrane glycoprotein with a signal peptide, an extracellular region, a transmembrane region, and a cytoplasmic domain. IL2RA is expressed on activated T cells and regulatory T cells and is capable of binding IL2 with low affinity by itself. However, a ligand-induced high-affinity heterotrimeric receptor complex is produced when IL2RA is associated non-covalently with the IL2 receptor beta and gamma chain, and subsequently initiates the intracellular signal pathways such as MAPK or JAK/STAT. On dendritic cells (DC), CD25 has been previously regarded as an activation marker, while both murine and human DC can express CD25, they do not express the beta-chain of the IL-2 receptor, which is indispensable for the execution of IL-2 signaling. The IL2RA (CD25) gene is a substantial component of the high-affinity receptor molecule highly expressed by activated T lymphocytes. Recently, a piece of strong evidence was obtained for the involvement of IL-2RA in conferring susceptibility to type 1 diabetes (T1D). Cancer growth and development are associated with the stimulation of the innate immune system, including enhanced interleukin 2 receptor (IL-2R) expression in immune cells and its shedding into the circulation in a soluble form of SIL-2Ralpha. In most hematological malignancies, including different types of leukemias and lymphomas, SIL-2Ralpha is released directly from the surface of neoplastic cells thus reflecting the tumor bulk, turnover, and activity. Several studies have proved that not only lymphoid cancer cells but also some non-lymphoid cancer cells, express IL-2R on their surface. They include malignant melanoma and carcinomas of the kidney, head and neck, esophagus, and lung. Thus, sIL-2Ralpha is elevated in most proliferative disturbances of the hematopoietic system and many solid tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPK-01071 | IL-22RA1 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Interleukin (IL)-22 is a member of the IL-10 family of cytokines and represents an important effector molecule of activated Th22, Th1, and Th17 cells, as well as Tc-cell subsets, gammadelta T cells, natural killer (NK), and NKT cells. IL-22 mediates its effects via a heterodimeric transmembrane receptor complex consisting of IL-22R1 and IL-10R2 and subsequent Janus kinase-signal transducers and activators of transcription (JAK-STAT) signaling pathways including Jak1, Tyk2, and STAT3.
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TMPK-00342 | IFNAR1 Protein, Mouse, Recombinant (His & Avi) | Mouse | HEK293 | ||
IFN-alpha / beta R1, also known as IFNAR1, belongs to the class II cytokine receptor family of proteins. Class II cytokine receptors form heterodimeric receptor complexes that mediate class II cytokine signals. Subunits of the different receptor complexes are shared and serve multiple functions.Functions in general as heterodimer with IFNAR2. Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves.
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TMPK-00343 | IFNAR1 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
IFN-alpha / beta R1, also known as IFNAR1, belongs to the class II cytokine receptor family of proteins. Class II cytokine receptors form heterodimeric receptor complexes that mediate class II cytokine signals. Subunits of the different receptor complexes are shared and serve multiple functions.Functions in general as heterodimer with IFNAR2. Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves.
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TMPK-00325 | IFNAR1 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
IFN-alpha / beta R1, also known as IFNAR1, belongs to the class II cytokine receptor family of proteins. Class II cytokine receptors form heterodimeric receptor complexes that mediate class II cytokine signals. Subunits of the different receptor complexes are shared and serve multiple functions.Functions in general as heterodimer with IFNAR2. Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves.
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TMPH-00779 | IL-23 P19/IL23A Protein, Guinea Pig, Recombinant (His & Myc) | Guinea pig | E. coli | ||
Associates with IL12B to form the IL-23 interleukin, a heterodimeric cytokine which functions in innate and adaptive immunity. IL-23 may constitute with IL-17 an acute response to infection in peripheral tissues. IL-23 binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R, activates the Jak-Stat signaling cascade, stimulates memory rather than naive T-cells and promotes production of proinflammatory cytokines. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and may be important for tumorigenesis.
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TMPK-00326 | IFNAR1, Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
IFN-alpha / beta R1, also known as IFNAR1, belongs to the class II cytokine receptor family of proteins. Class II cytokine receptors form heterodimeric receptor complexes that mediate class II cytokine signals. Subunits of the different receptor complexes are shared and serve multiple functions.Functions in general as heterodimer with IFNAR2. Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves.
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TMPK-01105 | IL-22RA1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Interleukin (IL)-22 is a member of the IL-10 family of cytokines and represents an important effector molecule of activated Th22, Th1, and Th17 cells, as well as Tc-cell subsets, gammadelta T cells, natural killer (NK), and NKT cells. IL-22 mediates its effects via a heterodimeric transmembrane receptor complex consisting of IL-22R1 and IL-10R2 and subsequent Janus kinase-signal transducers and activators of transcription (JAK-STAT) signaling pathways including Jak1, Tyk2, and STAT3.
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TMPU-00003 | STAT2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Signal transducer and activator of transcription that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state.
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TMPK-00575 | IL-23R Protein, Canine, Recombinant (His) | Canine | HEK293 | ||
Interleukin 23 (IL-23) is a heterodimeric cytokine composed of two disulfide-linked subunits, a p19 subunit that is unique to IL-23, and a p40 subunit that is shared with IL-12. The functional IL-23 receptor complex consists of two receptor subunits, the IL-12 receptor beta 1 subunit (IL-12 R beta 1) and the IL-23-specific receptor subunit (IL-23 R).This receptor associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade.
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TMPJ-00076 | IL-28B Protein, Human, Recombinant | Human | Human Cells | ||
Interleukin-28B, also known as Cytokine Zcyto22, Interferon lambda-3, Interferon lambda-4, IFNL3, IFNL4, ZCYTO22 and IL28B, is a secreted cytokine which belongs to the IL-28/IL-29 family. IL-28 has also been shown to play a role in the adaptive immune response. IL28B has immunomodulatory activity and up-regulates MHC class I antigen expression. IL28B displays potent antiviral activity and antitumor activity. In addition, IL28B is a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IL28RA. The ligand/receptor complex seems to signal through the Jak-STAT pathway.
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TMPK-01094 | IL-23R Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Interleukin 23 (IL-23) is a heterodimeric cytokine composed of two disulfide-linked subunits, a p19 subunit that is unique to IL-23, and a p40 subunit that is shared with IL-12. The functional IL-23 receptor complex consists of two receptor subunits, the IL-12 receptor beta 1 subunit (IL-12 R beta 1) and the IL-23-specific receptor subunit (IL-23 R).This receptor associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade.
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TMPK-00353 | IL-23R Protein, Human, Recombinant (aa 24-355, His) | Human | HEK293 | ||
Interleukin 23 (IL-23) is a heterodimeric cytokine composed of two disulfide-linked subunits, a p19 subunit that is unique to IL-23, and a p40 subunit that is shared with IL-12. The functional IL-23 receptor complex consists of two receptor subunits, the IL-12 receptor beta 1 subunit (IL-12 R beta 1) and the IL-23-specific receptor subunit (IL-23 R).This receptor associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade.
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TMPK-00652 | IL-23R Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Interleukin 23 (IL-23) is a heterodimeric cytokine composed of two disulfide-linked subunits, a p19 subunit that is unique to IL-23, and a p40 subunit that is shared with IL-12. The functional IL-23 receptor complex consists of two receptor subunits, the IL-12 receptor beta 1 subunit (IL-12 R beta 1) and the IL-23-specific receptor subunit (IL-23 R).This receptor associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade.
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TMPY-01489 | IFNAR1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Interferon-alpha/beta receptor alpha chain (IFNAR1) is a type I membrane protein that forms one of the two chains of a receptor for interferons alpha and beta. Binding and activation of the receptor stimulate Janus protein kinases, which in turn phosphorylate several proteins, including STAT1 and STAT2. The encoded protein also functions as an antiviral factor. Tyk2 slows down IFNAR1 degradation and that this is due, at least in part, to inhibition of IFNAR1 endocytosis. Mutant versions of IFNAR1, in which Tyr466 is changed to phenylalanine, can act in a dominant-negative manner to inhibit phosphorylation of STAT2. These observations are consistent with a model in which IFNAR1 mediates the interaction between JAK kinases and the STAT transcription factors.
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TMPY-02634 | IFNAR1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Interferon-alpha/beta receptor alpha chain (IFNAR1) is a type I membrane protein that forms one of the two chains of a receptor for interferons alpha and beta. Binding and activation of the receptor stimulate Janus protein kinases, which in turn phosphorylate several proteins, including STAT1 and STAT2. The encoded protein also functions as an antiviral factor. Tyk2 slows down IFNAR1 degradation and that this is due, at least in part, to inhibition of IFNAR1 endocytosis. Mutant versions of IFNAR1, in which Tyr466 is changed to phenylalanine, can act in a dominant-negative manner to inhibit phosphorylation of STAT2. These observations are consistent with a model in which IFNAR1 mediates the interaction between JAK kinases and the STAT transcription factors.
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TMPH-02156 | SOCS1 Protein, Human, Recombinant (His) | Human | Yeast | ||
SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS1 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Through binding to JAKs and IFNGR1, inhibits their kinase activity. In vitro, also suppresses Tec protein-tyrosine activity. Appears to be a major regulator of signaling by interleukin 6 (IL6) and leukemia inhibitory factor (LIF). Regulates interferon-gamma mediated sensory neuron survival. Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Seems to recognize JAK2. SOCS1 appears to be a negative regulator in IGF1R signaling pathway.
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TMPY-03829 | IFNAR1 Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
Interferon-alpha/beta receptor alpha chain (IFNAR1) is a type I membrane protein that forms one of the two chains of a receptor for interferons alpha and beta. Binding and activation of the receptor stimulate Janus protein kinases, which in turn phosphorylate several proteins, including STAT1 and STAT2. The encoded protein also functions as an antiviral factor. Tyk2 slows down IFNAR1 degradation and that this is due, at least in part, to inhibition of IFNAR1 endocytosis. Mutant versions of IFNAR1, in which Tyr466 is changed to phenylalanine, can act in a dominant-negative manner to inhibit phosphorylation of STAT2. These observations are consistent with a model in which IFNAR1 mediates the interaction between JAK kinases and the STAT transcription factors.
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