目录号 | 产品详情 | 靶点 | |
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T35664 | Others | ||
Tetracosactide acetate 是一种合成的多肽,可刺激肾上腺释放皮质类固醇 ,如皮质醇。Tetracosactide acetate 在溃疡性结肠炎和克罗恩病、青少年和成人类风湿性关节炎和骨关节病方面有研究的价值。 | |||
T10722 | Bombesin Receptor | ||
CD80-IN-3 是一种CD80抑制剂,抑制 CD80/CD28 互作的EC50=630 nM,Kd=125 nM。 | |||
T7527 | Beta Amyloid | ||
Frentizole 是一种 FDA 批准的免疫抑制剂,是一种新型 Aβ-ABAD 相互作用抑制剂。 | |||
T12783 | Integrin | ||
RWJ 50271 是具有口服活性的选择性LFA-1/ICAM-1相互作用抑制剂,抑制 LFA-1/ICAM-1 介导的细胞粘附,在细胞HL60中的IC50值为 5.0 μM。 | |||
T9706 | BTK | ||
BTK inhibitor 17 是口服有效的、不可逆的BTK 抑制剂,IC50为 2.1 nM。BTK inhibitor 17在类风湿关节炎方面有研究的价值。 | |||
T1421 | COX | ||
Aceclofenac (Preservex) 是一种可口服的非甾体抗炎药,可用于缓解疼痛、骨关节炎、强直性脊柱炎、类风湿性关节炎的研究。 | |||
T9911 | Interleukin | ||
Tocilizumab 是抗人白细胞介素-6 受体 (IL-6R) 的中和抗体,能够阻碍 IL-6 与 IL-6R 的结合,进而抑制经典和反式信号。它可用于研究类风湿性关节炎,对重症 COVID-19 冠状病毒病方面的研究具有显著效果。 | |||
T1846 | IL Receptor Lipase Interleukin | ||
Y-320 是一种免疫调节剂,能阻碍IL-15刺激CD4 T 细胞后的IL-17的产生,IC50=20~60 nM。 | |||
T11699 | CCR | ||
J-113863 是选择性的 CCR1 (CD18)拮抗剂,有抗炎作用,对人和小鼠 CCR1受体的 IC50值分别为 0.9 和 5.8 nM。它是人 CCR3的强效拮抗剂,还是小鼠 CCR3的弱效拮抗剂,IC50分别为 0.58 和 460 nM。 | |||
T13951 | TNF | ||
UCB-9260 是口服活性小分子,通过稳定三聚体的不对称形式抑制肿瘤坏死因子信号传导。它对肿瘤坏死因子的选择性高于其他超家族成员,并与肿瘤坏死因子结合,其Kd 值为 13 nM。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPJ-00995 | Serpin H1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Serpin H1 is a serine proteinase inhibitors Which belongs to the serpin family. Serpin H1 is induced by heat shock. Serpin H1 localizes to the endoplasmic reticulum lumen and binds specifically to collagen. Thus it is thought to be a molecular chaperone involved in the maturation of collagen molecules. Autoantibodies to this protein have been found in patients with rheumatoid arthritis. Serpin H1 may be a marker for cancer and nucleotide polymorphisms in this gene may be associated with preterm birth caused by preterm premature rupture of membranes.
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TMPJ-01172 | IL-17 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. Mature mouse IL-17A shares 61% and 89% amino acid sequence identity with human and rat IL-17A, respectively. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.
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TMPY-02970 | CXCL10 Protein, Human, Recombinant | Human | E. coli | ||
(C-X-C motif) ligand (CXCL)10 (CXCL10) belongs to the ELR(-) CXC subfamily chemokine. CXCL10/IP-10 exerts its function through binding to chemokine (C-X-C motif) receptor 3 (CXCR3), a seven trans-membrane receptor coupled to G proteins. CXCL10/IP-10 and its receptor, CXCR3, appear to contribute to the pathogenesis of many autoimmune diseases, organ specific (such as type 1 diabetes, autoimmune thyroiditis, Graves' disease and ophthalmopathy), or systemic (such as rheumatoid arthritis, psoriatic arthritis, systemic lupus erythematosus, mixed cryoglobulinemia, Sjögren syndrome, or systemic sclerosis). CXCL10/IP-10 is secreted by several cell types including endothelial cells, fibroblasts, keratinocytes, thyrocytes, preadipocytes, etc. Determination of high level of CXCL10/IP-10 in peripheral fluids is therefore a marker of host immune response.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01827 | CD30/TNFRSF8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor (TNFR) superfamily. CD30 protein is expressed by activated, but not resting, T and B cells. CD30 can regulate proliferation of lymphocytes and may also play an important role in human immunodeficiency virus replication. As a regulator of apoptosis, CD30 protein induces cell death or proliferation, depending on the cell type, and has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. CD30 protein expression is upregulated in various hematological malignancies, including Reed-Sternberg cells in Hodgkin's disease (HD), anaplastic large cell lymphoma (ALCL) and subsets of Non-Hodgkin's lymphomas (NHLs), and CD30 is also linked to leukocytes in patients with chronic inflammatory diseases, including lupus erythematosus, asthma, rheumatoid arthritis and atopic dermatitis (AD).Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-01371 | IL-17RA Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin-17 receptor (IL-17R), also known as Interleukin-17 receptor A (IL-17RA) and CD217 antigen (CD217), is a cytokine receptor that binds interleukin 17. IL-17R/IL-17RA (CD217) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. IL-17R/IL-17RA (CD217) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor IL-17RA play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Defects in IL-17R/IL-17RA (CD217) are the cause of familial candidiasis type 5 (CANDF5). CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails, and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.
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TMPY-02886 | IL-17A Protein, Human, Recombinant | Human | E. coli | ||
IL17, also known as IL17a, is a cytokine that belongs to the IL-17 family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation, and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. The IL-17 family of cytokines includes six members, IL-17/IL-17A, IL-17B, IL-17C, IL-17D, IL-17E/IL-25, and IL-17F, which are produced by multiple cell types. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. This cytokine can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis, and multiple sclerosis.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02900 | IL-17A Protein, Mouse, Recombinant | Mouse | E. coli | ||
IL17, also known as IL17a, is a cytokine that belongs to the IL-17 family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation, and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. The IL-17 family of cytokines includes six members, IL-17/IL-17A, IL-17B, IL-17C, IL-17D, IL-17E/IL-25, and IL-17F, which are produced by multiple cell types. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. This cytokine can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis, and multiple sclerosis.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00021 | PADI4 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Protein-arginine deiminase type-4, also known as HL-6 PAD, Peptidylarginine deiminase IV, Protein-arginine deiminase type I V and PADI4, is a cytoplasm and nucleus protein that belongs to the protein arginine deiminase family. PADI4 is expressed in CD34+stem cells in normal tissues, and many more CD34+ cells expressing PADI4 are present in tumour tissues. PADI4 post-translationally converts peptidylarginine to citrulline, a process called citrullination. Studies have demonstrated the high expression of PADI4 in various malignant tumor tissues. PADI4 is also expressed at high levels in the blood of patients with some malignant tumors. Citrullination of histone, cytokeratin, antithrombin and fibronectin have been confirmed to be involved in abnormal apoptosis, high coagulation, and disordered cell proliferation and differentiation, all of which are main features of malignant tumors. PADI4 may play an important role in tumorigenesis. Genetic variations in PADI4 are a cause of susceptibility to rheumatoid arthritis (RA). It is a systemic inflammatory disease with autoimmune features and a complex genetic component. It primarily affects the joints and is characterized by inflammatory changes in the synovial membranes and articular structures, widespread fibrinoid degeneration of the collagen fibers in mesenchymal tissues, and by atrophy and rarefaction of bony structures.
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TMPJ-00042 | TSLP Protein, Human, Recombinant | Human | E. coli | ||
Thymic stromal lymphopoietin (TSLP) is a novel member of the hemopoietic cytokine family that promotes the development of B cells and shares overlapping activity with IL-7. The human TSLP protein comprises a 28 amino acids (aa) signal sequence and 131 aa mature region. Human TSLP has two isoforms lfTSLP and sfTSLP produced by alternative splicing . lfTSLP is expressed in a number of tissues including heart, liver and prostate, and sfTSLP (63aa) is predominantly expressed in keratinocytes of oral mucosa, skin and in salivary glands. In aa sequence level, Human TSLP displays about 43% identity with mouse TSLP.TSLP is a cytokine that functions mainly on myeloid cells; it induces the release of T cell-attracting chemokines from monocytes and enhances the maturation of CD11c(+) dendritic cells.TSLP has proliferative effects on the myeloid cell line and may initiate asthma or atopic dermatitis responses by directly activating mast cells . TSLP signals cells via the interleukin-7 receptor-α chain (IL-7Rα),shared with IL-7, together with the TSLP receptor (TSLPR) subunit. Recent studies indicate that TSLP and its receptor are novel therapeutic targets for rheumatoid arthritis,for increased intraarticular TSLP concentrations in patients has caused chemotaxis and activation of arthritogenic T cells.
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TMPY-00740 | SDF-1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPY-02590 | HMGB1 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
High-mobility group box 1 protein (HMGB1), also known as HMG-1 or amphoterin previously, is a member of the HMGB family consisting of three members, HMGB1, HMGB2, and HMGB3. HMGB1 is a DNA-binding nuclear protein, released actively following cytokine stimulation as well as passively during cell death. It is the prototypic damage-associated molecular pattern (DAMP) molecule and has been implicated in several inflammatory disorders. HMGB1 signals via the receptor for advanced glycation end-product (RAGE) and members of the toll-like receptor (TLR) family. The most prominent HMGB1 protein and mRNA expression arthritis are present in pannus regions, where synovial tissue invades articular cartilage and bone. HMGB1 promotes the activity of proteolytic enzymes, and osteoclasts need HMGB1 for functional maturation. As a non-histone nuclear protein, HMGB1 has a dual function. Inside the cell, HMGB1 binds DNA, regulating transcription, and determining chromosomal architecture. Outside the cell, HMGB1 can serve as an alarmin to activate the innate system and mediate a wide range of physiological and pathological responses. Extracellular HMGB1 represents an optimal " necrotic marker" selected by the innate immune system to recognize tissue damage and initiate reparative responses. However, extracellular HMGB1 also acts as a potent pro-inflammatory cytokine that contributes to the pathogenesis of diverse inflammatory and infectious disorders. HMGB1 has been successfully therapeutically targeted in multiple preclinical models of infectious and sterile diseases including arthritis. As shown in studies on patients as well as animal models, HMGB1 can play an important role in the pathogenesis of the rheumatic disease, including rheumatoid arthritis, systemic lupus erythematosus, and polymyositis among others. Besides, enhanced postmyocardial infarction remodeling in type 1 diabetes mellitus was partially mediated by HMGB1 activation.
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TMPY-02591 | SDF-1 Protein, Human, Recombinant | Human | E. coli | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPY-02820 | SDF-1 Protein, Human, Recombinant (isoform a) | Human | E. coli | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPY-01848 | HMGB1 Protein, Human, Recombinant (aa 1-215, His) | Human | HEK293 | ||
High-mobility group box 1 protein (HMGB1), also known as HMG-1 or amphoterin previously, is a member of the HMGB family consisting of three members, HMGB1, HMGB2, and HMGB3. HMGB1 is a DNA-binding nuclear protein, released actively following cytokine stimulation as well as passively during cell death. It is the prototypic damage-associated molecular pattern (DAMP) molecule and has been implicated in several inflammatory disorders. HMGB1 signals via the receptor for advanced glycation end-product (RAGE) and members of the toll-like receptor (TLR) family. The most prominent HMGB1 protein and mRNA expression arthritis are present in pannus regions, where synovial tissue invades articular cartilage and bone. HMGB1 promotes the activity of proteolytic enzymes, and osteoclasts need HMGB1 for functional maturation. As a non-histone nuclear protein, HMGB1 has a dual function. Inside the cell, HMGB1 binds DNA, regulating transcription, and determining chromosomal architecture. Outside the cell, HMGB1 can serve as an alarmin to activate the innate system and mediate a wide range of physiological and pathological responses. Extracellular HMGB1 represents an optimal " necrotic marker" selected by the innate immune system to recognize tissue damage and initiate reparative responses. However, extracellular HMGB1 also acts as a potent pro-inflammatory cytokine that contributes to the pathogenesis of diverse inflammatory and infectious disorders. HMGB1 has been successfully therapeutically targeted in multiple preclinical models of infectious and sterile diseases including arthritis. As shown in studies on patients as well as animal models, HMGB1 can play an important role in the pathogenesis of the rheumatic disease, including rheumatoid arthritis, systemic lupus erythematosus, and polymyositis among others. Besides, enhanced postmyocardial infarction remodeling in type 1 diabetes mellitus was partially mediated by HMGB1 activation.
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TMPY-04902 | Complement C5a Protein, Mouse, Recombinant | Mouse | E. coli | ||
C5a is a protein fragment released from complement component C5. This 74 amino acid peptide in humans is generated by the cleavage of C5a convertase on the C5 α-chain during the classical, alternative, and lectin pathways of complement activation. The structure of C5a includes a core region consisting of four, anti-parallel alpha-helices held together by three disulfide linkages and a structured C-terminal tail, and C5a is rapidly metabolised by carboxypeptidase B to a 73 amino acid low activity form, C5a des-Arg. C5a is an extremely potent proinflammatory mediator, as well as a potent chemotactic factor for neutrophils and other leukocytes. It causes histamine release, increases in vascular permeability, induces several cytokines production from leukocytes, enhances neutrophil-endothelial cell adhesion, and augments the humoral and cell-mediated immune response. C5a is quickly metabolised by carboxypeptidases, forming the less potent C5adesArg. Acting via a classical G protein-coupled receptor, CD88, C5a and C5adesArg exert a number of effects essential to the innate immune response, while their actions at the more recently discovered non-G protein-coupled receptor, C5L2 (or GPR77), remain unclear. The widespread expression of C5a receptors throughout the body allows C5a to elicit a broad range of effects. Thus, C5a has been found to be a significant pathogenic driver in a number of immuno-inflammatory diseases, making C5a inhibition an attractive therapeutic strategy. C5a is a strong chemoattractant and is involved in the recruitment of inflammatory cells such as neutrophils, eosinophils, monocytes, and T lymphocytes, in activation of phagocytic cells and release of granule-based enzymes and generation of oxidants, all of which may contribute to innate immune functions or tissue damage. Accordingly, the anaphylatoxin C5a is implicated in a variety of diseases such as rheumatoid arthritis, systemic lupus erythematosus, reperfusion injury, Alzheimer's disease, and sepsis.
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TMPY-05057 | Complement C5 Protein, Human, Recombinant (His & FLAG) | Human | HEK293 | ||
C5a is a protein fragment released from complement component C5. This 74 amino acid peptide in humans is generated by the cleavage of C5a convertase on the C5 α-chain during the classical, alternative, and lectin pathways of complement activation. The structure of C5a includes a core region consisting of four, anti-parallel alpha-helices held together by three disulfide linkages and a structured C-terminal tail, and C5a is rapidly metabolised by carboxypeptidase B to a 73 amino acid low activity form, C5a des-Arg. C5a is an extremely potent proinflammatory mediator, as well as a potent chemotactic factor for neutrophils and other leukocytes. It causes histamine release, increases in vascular permeability, induces several cytokines production from leukocytes, enhances neutrophil-endothelial cell adhesion, and augments the humoral and cell-mediated immune response. C5a is quickly metabolised by carboxypeptidases, forming the less potent C5adesArg. Acting via a classical G protein-coupled receptor, CD88, C5a and C5adesArg exert a number of effects essential to the innate immune response, while their actions at the more recently discovered non-G protein-coupled receptor, C5L2 (or GPR77), remain unclear. The widespread expression of C5a receptors throughout the body allows C5a to elicit a broad range of effects. Thus, C5a has been found to be a significant pathogenic driver in a number of immuno-inflammatory diseases, making C5a inhibition an attractive therapeutic strategy. C5a is a strong chemoattractant and is involved in the recruitment of inflammatory cells such as neutrophils, eosinophils, monocytes, and T lymphocytes, in activation of phagocytic cells and release of granule-based enzymes and generation of oxidants, all of which may contribute to innate immune functions or tissue damage. Accordingly, the anaphylatoxin C5a is implicated in a variety of diseases such as rheumatoid arthritis, systemic lupus erythematosus, reperfusion injury, Alzheimer's disease, and sepsis.
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TMPY-00653 | Complement C5 Protein, Human, Recombinant (Complement C5a) | Human | E. coli | ||
C5a is a protein fragment released from complement component C5. This 74 amino acid peptide in humans is generated by the cleavage of C5a convertase on the C5 α-chain during the classical, alternative, and lectin pathways of complement activation. The structure of C5a includes a core region consisting of four, anti-parallel alpha-helices held together by three disulfide linkages and a structured C-terminal tail, and C5a is rapidly metabolised by carboxypeptidase B to a 73 amino acid low activity form, C5a des-Arg. C5a is an extremely potent proinflammatory mediator, as well as a potent chemotactic factor for neutrophils and other leukocytes. It causes histamine release, increases in vascular permeability, induces several cytokines production from leukocytes, enhances neutrophil-endothelial cell adhesion, and augments the humoral and cell-mediated immune response. C5a is quickly metabolised by carboxypeptidases, forming the less potent C5adesArg. Acting via a classical G protein-coupled receptor, CD88, C5a and C5adesArg exert a number of effects essential to the innate immune response, while their actions at the more recently discovered non-G protein-coupled receptor, C5L2 (or GPR77), remain unclear. The widespread expression of C5a receptors throughout the body allows C5a to elicit a broad range of effects. Thus, C5a has been found to be a significant pathogenic driver in a number of immuno-inflammatory diseases, making C5a inhibition an attractive therapeutic strategy. C5a is a strong chemoattractant and is involved in the recruitment of inflammatory cells such as neutrophils, eosinophils, monocytes, and T lymphocytes, in activation of phagocytic cells and release of granule-based enzymes and generation of oxidants, all of which may contribute to innate immune functions or tissue damage. Accordingly, the anaphylatoxin C5a is implicated in a variety of diseases such as rheumatoid arthritis, systemic lupus erythematosus, reperfusion injury, Alzheimer's disease, and sepsis.
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TMPJ-01444 | IL-17A Protein, Cynomolgus, Recombinant (His) | Cynomolgus | Human Cells | ||
Interleukin-17 is a potent pro-inflammatory cytokine produced by activated memory T cells. There are at least six members of the IL-17 family in humans and in mice. As IL-17 shares properties with IL-1 and TNF-alpha, it may induce joint inflammation and bone and cartilage destruction. This cytokine is found in synovial fluids of patients with rheumatoid arthritis, and produced by rheumatoid arthritis synovium. It increases IL-6 production, induces collagen degradation and decreases collagen synthesis by synovium and cartilage and proteoglycan synthesis in cartilage. IL-17 is also able to increase bone destruction and reduce its formation. Blocking of interleukin-17 with specific inhibitors provides a protective inhibition of cartilage and bone degradation.
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TMPK-01329 | ANGPTL4 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Candidates for this common regulatory system include signals mediated by peroxisome proliferator-activated regulator and its response factor, angiopoietin-like 4. The expression and bioactivity of angiopoietin-like 4, an adipocytokine that was originally reported to have an angiogenic function, have been detected not only in the vascular system and adipose tissue but also in rheumatoid joints.
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TMPK-01092 | OSCAR Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Osteoclast-associated receptor (OSCAR) is a co-stimulatory receptor in osteoclastogenesis. Synovial tissues from active rheumatoid arthritis (RA) patients express higher levels of OSCAR compared with osteoarthritic and normal patients. OSCAR and tartrate-resistant acid phosphatase (TRAP) expression levels did not differ between the cartilage pannus junction (CPJ) and non-CPJ regions in active RA.
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TMPK-01117 | OSCAR Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Osteoclast-associated receptor (OSCAR) is a co-stimulatory receptor in osteoclastogenesis. Synovial tissues from active rheumatoid arthritis (RA) patients express higher levels of OSCAR compared with osteoarthritic and normal patients. OSCAR and tartrate-resistant acid phosphatase (TRAP) expression levels did not differ between the cartilage pannus junction (CPJ) and non-CPJ regions in active RA.
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TMPJ-00191 | FSTL1 Protein, Human, Recombinant | Human | E. coli | ||
Follistatin-Related Protein 1 (FSTL1) is a secreted protein that contains two EF-hand domains, one follistatin-like domain, one Kazal-like domain, and one VWFC domain. Its functional significance in physiological and pathological processes is not completely understood. However, FSTL1 is thought to modulate the action of some growth factors on cell proliferation and differentiation. FSTL1 maybe an autoantigen associated with rheumatoid arthritis.
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TMPK-00172 | B7-H4 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
B7-H4, also known as B7x and B7S1, is a 50-80 kDa glycosylated member of the B7 family of immunomodulatory proteins.B7-H4 is up-regulated in several carcinomas in correlation with tumor progression and metastasis. A soluble form of B7-H4 is elevated in the serum of ovarian cancer, renal cell carcinoma, and rheumatoid arthritis patients, also in correlation with advanced disease status .
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TMPJ-00532 | PADI4 Protein, Human, Recombinant (E. coli, His) | Human | E. coli | ||
Protein-Arginine Deiminase Type-4 (PADI4) belongs to the Protein Arginine Deiminase family. PADI4 is expressed in eosinophils and neutrophils, but it is not expressed in peripheral monocytes or lymphocytes. PADI4 catalyzes the citrullination/deimination of arginine residues of proteins. In addition, PADI4 may play an important role in tumourigenesis. Genetic variations in PADI4 are a cause of susceptibility to rheumatoid arthritis (RA), which is a systemic inflammatory disease with autoimmune features and a complex genetic component.
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TMPJ-01312 | TWEAKR/TNFRSF12A Protein, Mouse, Recombinant (hFc) | Mouse | Human Cells | ||
Tumor necrosis factor receptor superfamily member 12A(Tnfrsf12a) is a single-pass type I membrane protein and contains 1 TNFR-Cys repeat. It is weak inducer of apoptosis in some cell types.It promotes angiogenesis and it is the proliferation of endothelial cells. It may modulate cellular adhesion to matrix proteins.TNFR binds specifically to tumor necrosis factor (TNF) and blocks its interaction with cell surface TNF receptors. TNF is a naturally occurring cytokine that is involved in normal inflammatory and immune responses. It plays an important role in the inflammatory processes of rheumatoid arthritis (RA), polyarticular-course juvenile rheumatoid arthritis (JRA), and ankylosing spondylitis and the resulting joint pathology. In addition, TNF plays a role in the inflammatory process of plaque psoriasis. Elevated levels of TNF are found in involved tissues and fluids of patients with RA, psoriatic arthritis, ankylosing spondylitis (AS), and plaque psoriasis. Two distinct receptors for TNF (TNFRs), a 55 kilodalton protein (p55) and a 75 kilodalton protein (p75), exist naturally as monomeric molecules on cell surfaces and in soluble forms. Biological activity of TNF is dependent upon binding to either cell surface TNFR.
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TMPJ-01110 | IRF5 Protein, Human, Recombinant (His) | Human | E. coli | ||
Interferon Regulatory Factor 5 (IRF5) is a member of the IRF family. It contains one IRF tryptophan pentad repeat DNA-binding domain. IRF5 shuttles between the nucleus and the cytoplasm. IRF5 can form homodimer when it is phosphorylated. IRF5 functions as a transcription factor involved in the induction of interferons IFNA and INFB and inflammatory cytokines upon virus infection. Genetic variations in IRF5 are associated with susceptibility to systemic lupus erythematosus type 10. In addition, the genetic variations wil result in susceptibility to rheumatoid arthritis.
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TMPJ-00658 | CYR61/CCN1 Protein, Human, Recombinant (hFc) | Human | Human Cells | ||
Protein CYR61, also known as CCN family member 1, Cysteine-rich angiogenic inducer 61,Insulin-like growth factor-binding protein 10 , GIG1, CYR61, CCN1 and IGFBP10, belongs to the CCN family, CYR61 is a secreted protein and contains one CTCK (C-terminal cystine knot-like) domain,one IGFBP N-terminal domain,one TSP type-1 domain and one VWFC domain. CYR61 promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. CYR61 plays important roles in inflammation and tissue repair. CYR61 is associated with diseases related to chronic inflammation, including rheumatoid arthritis, atherosclerosis, diabetes-related nephropathy and retinopathy, and many different forms of cancers.
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TMPK-01378 | IL-12B Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Interleukin (IL)‑12B, which encodes the p40 subunit common to IL‑12 and IL‑23, as one of the genes for which expression in fibroblast‑like synoviocytes from patients with rheumatoid arthritis (RA‑FLS) is induced by DcR3.Decoy receptor 3 (DcR3) competitively binds to three ligands, Fas ligand, lymphotoxin‑related inducible ligand that competes for glycoprotein D binding to herpesvirus entry mediator on T cells and tumor necrosis factor‑like ligand 1A (TL1A), to prevent their effects. Recent studies have suggested that DcR3 directly affects cells as a ligand.
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TMPJ-00202 | CD157 Protein, Human, Recombinant (hFc) | Human | Human Cells | ||
The cluster of differentiation (CD) system is a glycosyl phosphatidylinositol anchored membrane protein that belongs to the CD38 family.It is generally used in immunophynotyping. CD157 was discovered in a bone marrow stromal cell line where it facilitates pre-B-cell growth. CD157 is a bifunctional ectoenzyme that exhibits both ADP-ribosyl cyclase and cyclic ADP ribose hydrolase activities followed with CD38. It plays a role in rheumatoid arthritis (RA) due to its enhanced expression in RA-derived bone marrow stromal cell lines. Studies have shown that this protein have a role in predicted to function as a cell surface receptor and an immunoregulatory molecule.
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TMPJ-00621 | LILRB1/CD85j/ILT2 Protein, Rhesus macaque, Recombinant (aa 17-456, His) | Rhesus Macaque | Human Cells | ||
LILRB1, also known as CD85j and ILT2, is a transmembrane glycoprotein in the LILR immunoregulatory protein family. LILRB1 is expressed on NK cells that have expanded in response to acute HCMV infection. LILRB1 exhibits considerable diversity in the population, and polymorphisms in the LILRB1 gene have been associated with susceptibility to rheumatoid arthritis and weakly associated with HCMV disease in a subset of patients with HIV. The regulation of phagocytosis by macrophages is an additional key role of LILRB1 signaling. LILRB1 recognizes a wide variety of HLA haplotypes due to its interaction with the invariant β2M subunit of MHC class I, which suggests that this signaling axis is relevant across diverse patient populations.
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TMPY-02556 | FSTL1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Follistatin-related protein 1 (FSTL1) is an extracellular glycoprotein whose functional significance in physiological and pathological processes is incompletely understood. Recently, we have shown that FSTL1 acts as a muscle-derived secreted factor that is up-regulated by Akt activation and ischemic stress and that FSTL1 exerts favorable actions on the heart and vasculature. Here, we sought to identify the receptor that mediates the cellular actions of FSTL1. It contains an FS module, a follistatin-like sequence containing 10 conserved cysteine residues. FSTL1 is thought to be an autoantigen associated with rheumatoid arthritis. DIP2A functions as a novel receptor that mediates the cardiovascular protective effects of FSTL1. Experiment results have provided in vivo and in vitro evidence to demonstrate that Fstl1 modulates lung development and alveolar maturation, in part, through BMP4 signaling.
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TMPY-02817 | IL-1F8 Protein, Human, Recombinant (His) | Human | E. coli | ||
Interleukin-1 family member 8(IL1F8) also known as IL36B, is a member of the interleukin 1(IL-1) cytokine family. IL1F8 may contain a 12-stranded beta-trefoil structure. Until recently, the IL-1 family of cytokines includes four members, with three having pro-inflammatory effects such as IL1F8 and the fourth member being an IL-1 receptor antagonist (IL-1Ra). IL-1 family members exert their effects through binding to receptors that belong to the IL-1 receptor (IL-1R) family. IL1F8 exerts proinflammatory effects in primary human joint cells. Joint and serum IL-1F8 protein levels did not correlate with inflammation, but they were high in some human serum samples tested, including samples from patients with rheumatoid arthritis. IL1F8 also activated NK-κB.
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TMPY-02319 | Galectin-3 Protein, Human, Recombinant | Human | E. coli | ||
LGALS3 (Galectin 3) is a Protein Coding gene. This gene encodes a member of the galectin family of carbohydrate-binding proteins. The encoded protein is characterized by an N-terminal proline-rich tandem repeat domain and a single C-terminal carbohydrate recognition domain. LGALS3 is a beta-galactoside-binding lectin and plays a role in numerous cellular functions including apoptosis, innate immunity, cell adhesion, and T-cell regulation. LGALS3 has an important role in tumor progression through inhibition of apoptosis. LGALS3 expression is associated with neoplastic transformation and with differentiation of monocytes to macrophages. Elevated expression of LGALS3 has been demonstrated in the synovium of rheumatoid arthritis (RA). Diseases associated with LGALS3 include Follicular Adenoma and Papillary Carcinoma.
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TMPJ-00981 | PTX3 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Pentraxin-related protein PTX3, also known as Tumor necrosis factor-inducible gene 14 protein (TSG-14), belongs to the pentraxin family. PTX3 plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility. It’s subunit is a disulfide-linked homooctamer that binds to C1q. PTX3 concentration is elevated in the joint fluid of patients with rheumatoid arthritis (RA), indicating that PTX3 may be a potential mediator of immune response. PTX3 may also function in the regulation of the uptake and clearance of apoptotic cells by dendritic cells. An in vivo study showed that PTX3 transgenic mice are more resistant to sepsis and endotoxemia compared to wild-type during inflammatory injury.
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TMPY-02965 | MMP-19 Protein, Human, Recombinant | Human | E. coli | ||
MMP19, also known as RASI-1, is a member of the peptidase M1A family. It contains 4 hemopexin-like domains and is expressed in the mammary gland, placenta, lung, pancreas, ovary, small intestine, spleen, thymus, prostate, testis colon, heart, and blood vessel walls. It is a matrix metalloproteinase (MMP). Proteins of the MMP family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP19 may play a role in pathological processes participating in rheumatoid arthritis (RA)-associated joint tissue destruction. Autoantigen anti-MMP19 is frequent in RA patients.
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TMPY-00613 | FSTL1 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Follistatin-related protein 1 (FSTL1) is an extracellular glycoprotein whose functional significance in physiological and pathological processes is incompletely understood. Recently, we have shown that FSTL1 acts as a muscle-derived secreted factor that is up-regulated by Akt activation and ischemic stress and that FSTL1 exerts favorable actions on the heart and vasculature. Here, we sought to identify the receptor that mediates the cellular actions of FSTL1. It contains an FS module, a follistatin-like sequence containing 10 conserved cysteine residues. FSTL1 is thought to be an autoantigen associated with rheumatoid arthritis. DIP2A functions as a novel receptor that mediates the cardiovascular protective effects of FSTL1. Experiment results have provided in vivo and in vitro evidence to demonstrate that Fstl1 modulates lung development and alveolar maturation, in part, through BMP4 signaling.
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TMPY-04286 | IL-22RA1 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
IL-22R belongs to the type II cytokine receptor family. It contains 2 fibronectin type-III domains and is expressed in the colon, liver, lung, pancreas, and kidney. IL-22R also can be expressed in keratinocytes of normal skin as well as in psoriatic skin lesions. Overexpression of IL-22R can be detected in synovial fluid cells from rheumatoid arthritis and spondyloarthropathy patients. IL-22R is a component of the receptor for IL20, IL22, and IL24. The component of IL-22R formed by IL22RA1 and IL10RB enables IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptors for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. IL-22R mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation.
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TMPY-02458 | IL-1F8 Protein, Human, Recombinant | Human | E. coli | ||
Interleukin-1 family member 8(IL1F8) also known as IL36B, is a member of the interleukin 1(IL-1) cytokine family. IL1F8 may contain a 12-stranded beta-trefoil structure. Until recently, the IL-1 family of cytokines includes four members, with three having pro-inflammatory effects such as IL1F8 and the fourth member being an IL-1 receptor antagonist (IL-1Ra). IL-1 family members exert their effects through binding to receptors that belong to the IL-1 receptor (IL-1R) family. IL1F8 exerts proinflammatory effects in primary human joint cells. Joint and serum IL-1F8 protein levels did not correlate with inflammation, but they were high in some human serum samples tested, including samples from patients with rheumatoid arthritis. IL1F8 also activated NK-κB.
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TMPY-02583 | IL-1F8 Protein, Mouse, Recombinant | Mouse | E. coli | ||
Interleukin-1 family member 8(IL1F8) also known as IL36B, is a member of the interleukin 1(IL-1) cytokine family. IL1F8 may contain a 12-stranded beta-trefoil structure. Until recently, the IL-1 family of cytokines includes four members, with three having pro-inflammatory effects such as IL1F8 and the fourth member being an IL-1 receptor antagonist (IL-1Ra). IL-1 family members exert their effects through binding to receptors that belong to the IL-1 receptor (IL-1R) family. IL1F8 exerts proinflammatory effects in primary human joint cells. Joint and serum IL-1F8 protein levels did not correlate with inflammation, but they were high in some human serum samples tested, including samples from patients with rheumatoid arthritis. IL1F8 also activated NK-κB.
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TMPY-02952 | SIAE Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Sialate O-acetylesterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. It is widely expressed with high expression in the testis, prostate, and colon. The systematic name of this enzyme class is N-acyl-O-acetylneuraminate O-acetylhydrolase. Other names in common use include N-acetylneuraminate acetyltransferase, sialate 9(4)-O-acetylesterase, and sialidase. Sialate O-acetylesterase catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid. Defects in Sialate O-acetylesterase are a cause of autoimmune disease type 6 (AIS6). Individuals manifesting susceptibility to autoimmune disease type 6 can suffer from juvenile idiopathic arthritis, rheumatoid arthritis, multiple sclerosis, Sjogren syndrome, systemic lupus erythematosus, type 1 diabetes, ulcerative colitis, and Crohn disease.
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TMPY-01106 | FSTL1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Follistatin-related protein 1 (FSTL1) is an extracellular glycoprotein whose functional significance in physiological and pathological processes is incompletely understood. Recently, we have shown that FSTL1 acts as a muscle-derived secreted factor that is up-regulated by Akt activation and ischemic stress and that FSTL1 exerts favorable actions on the heart and vasculature. Here, we sought to identify the receptor that mediates the cellular actions of FSTL1. It contains an FS module, a follistatin-like sequence containing 10 conserved cysteine residues. FSTL1 is thought to be an autoantigen associated with rheumatoid arthritis. DIP2A functions as a novel receptor that mediates the cardiovascular protective effects of FSTL1. Experiment results have provided in vivo and in vitro evidence to demonstrate that Fstl1 modulates lung development and alveolar maturation, in part, through BMP4 signaling.
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TMPY-04943 | CXCL10 Protein, Rat, Recombinant (His) | Rat | Yeast | ||
(C-X-C motif) ligand (CXCL)10 (CXCL10) belongs to the ELR(-) CXC subfamily chemokine. CXCL10/IP-10 exerts its function through binding to chemokine (C-X-C motif) receptor 3 (CXCR3), a seven trans-membrane receptor coupled to G proteins. CXCL10/IP-10 and its receptor, CXCR3, appear to contribute to the pathogenesis of many autoimmune diseases, organ specific (such as type 1 diabetes, autoimmune thyroiditis, Graves' disease and ophthalmopathy), or systemic (such as rheumatoid arthritis, psoriatic arthritis, systemic lupus erythematosus, mixed cryoglobulinemia, Sjögren syndrome, or systemic sclerosis). CXCL10/IP-10 is secreted by several cell types including endothelial cells, fibroblasts, keratinocytes, thyrocytes, preadipocytes, etc. Determination of high level of CXCL10/IP-10 in peripheral fluids is therefore a marker of host immune response.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05118 | CD30/TNFRSF8 Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor (TNFR) superfamily. CD30 protein is expressed by activated, but not resting, T and B cells. CD30 can regulate proliferation of lymphocytes and may also play an important role in human immunodeficiency virus replication. As a regulator of apoptosis, CD30 protein induces cell death or proliferation, depending on the cell type, and has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. CD30 protein expression is upregulated in various hematological malignancies, including Reed-Sternberg cells in Hodgkin's disease (HD), anaplastic large cell lymphoma (ALCL) and subsets of Non-Hodgkin's lymphomas (NHLs), and CD30 is also linked to leukocytes in patients with chronic inflammatory diseases, including lupus erythematosus, asthma, rheumatoid arthritis and atopic dermatitis (AD).Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-06430 | CD30/TNFRSF8 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor (TNFR) superfamily. CD30 protein is expressed by activated, but not resting, T and B cells. CD30 can regulate proliferation of lymphocytes and may also play an important role in human immunodeficiency virus replication. As a regulator of apoptosis, CD30 protein induces cell death or proliferation, depending on the cell type, and has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. CD30 protein expression is upregulated in various hematological malignancies, including Reed-Sternberg cells in Hodgkin's disease (HD), anaplastic large cell lymphoma (ALCL) and subsets of Non-Hodgkin's lymphomas (NHLs), and CD30 is also linked to leukocytes in patients with chronic inflammatory diseases, including lupus erythematosus, asthma, rheumatoid arthritis and atopic dermatitis (AD).Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPJ-00698 | BTNL2 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Butyrophilin-like 2 (BTNL2) is a member of the BTN/MOG Ig-superfamily and functions as a negative regulator of immune cell activation. Mouse BTNL2 is type I transmembrane glycoprotein that contains an extracellular domain (ECD), a transmembrane region and a short cytoplasmic domain. The ECD features two V-type Ig-like domains, two C-type Ig-like domains, and four glycosylation sites. BTNL2 is expressed in epithelial cells of the small intestine, colonic dendritic cells, and in cells of the lymph node. BTNL2 expression is upregulated in T cells following activation, a characteristic BTNL2 shares with the homologous B7 family of costimulatory molecules. BTNL2 negatively regulates T cells by inhibiting proliferation and inflammatory cytokine secretion. It also increases the expression of FoxP3 in T cells to promote regulatory T cell development. Single nucleotide polymorphisms in BTNL2 are associated with a risk for sporadic prostate cancer, rheumatoid arthritis, sarcoidosis, ulcerative colitis, and other inflammatory diseases.
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TMPY-05471 | CD30/TNFRSF8 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor (TNFR) superfamily. CD30 protein is expressed by activated, but not resting, T and B cells. CD30 can regulate proliferation of lymphocytes and may also play an important role in human immunodeficiency virus replication. As a regulator of apoptosis, CD30 protein induces cell death or proliferation, depending on the cell type, and has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. CD30 protein expression is upregulated in various hematological malignancies, including Reed-Sternberg cells in Hodgkin's disease (HD), anaplastic large cell lymphoma (ALCL) and subsets of Non-Hodgkin's lymphomas (NHLs), and CD30 is also linked to leukocytes in patients with chronic inflammatory diseases, including lupus erythematosus, asthma, rheumatoid arthritis and atopic dermatitis (AD).Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05737 | CD30/TNFRSF8 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor (TNFR) superfamily. CD30 protein is expressed by activated, but not resting, T and B cells. CD30 can regulate proliferation of lymphocytes and may also play an important role in human immunodeficiency virus replication. As a regulator of apoptosis, CD30 protein induces cell death or proliferation, depending on the cell type, and has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. CD30 protein expression is upregulated in various hematological malignancies, including Reed-Sternberg cells in Hodgkin's disease (HD), anaplastic large cell lymphoma (ALCL) and subsets of Non-Hodgkin's lymphomas (NHLs), and CD30 is also linked to leukocytes in patients with chronic inflammatory diseases, including lupus erythematosus, asthma, rheumatoid arthritis and atopic dermatitis (AD).Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-04087 | IL-22RA1 Protein, Canine, Recombinant (His) | Canine | HEK293 | ||
IL-22R belongs to the type II cytokine receptor family. It contains 2 fibronectin type-III domains and is expressed in the colon, liver, lung, pancreas, and kidney. IL-22R also can be expressed in keratinocytes of normal skin as well as in psoriatic skin lesions. Overexpression of IL-22R can be detected in synovial fluid cells from rheumatoid arthritis and spondyloarthropathy patients. IL-22R is a component of the receptor for IL20, IL22, and IL24. The component of IL-22R formed by IL22RA1 and IL10RB enables IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptors for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. IL-22R mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation.
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TMPY-06282 | CD30/TNFRSF8 Protein, Human, Recombinant (hFc & Avi), Biotinylated | Human | HEK293 | ||
CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor (TNFR) superfamily. CD30 protein is expressed by activated, but not resting, T and B cells. CD30 can regulate proliferation of lymphocytes and may also play an important role in human immunodeficiency virus replication. As a regulator of apoptosis, CD30 protein induces cell death or proliferation, depending on the cell type, and has been shown to limit the proliferative potential of autoreactive CD8 effector T cells and protect the body against autoimmunity. CD30 protein expression is upregulated in various hematological malignancies, including Reed-Sternberg cells in Hodgkin's disease (HD), anaplastic large cell lymphoma (ALCL) and subsets of Non-Hodgkin's lymphomas (NHLs), and CD30 is also linked to leukocytes in patients with chronic inflammatory diseases, including lupus erythematosus, asthma, rheumatoid arthritis and atopic dermatitis (AD).Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00725 | COMP Protein, Human, Recombinant (His) | Human | HEK293 | ||
Cartilage Oligomeric Matrix Protein (COMP), also referred to as Thrombospondin-5, is a non-collagenous extracellular matrix (ECM) protein and belongs to the subgroup B of the thrombospondin protein family. This protein is expressed primarily in cartilage, ligament, and tendon, and binds to other ECM proteins such as collagen I, II and IX with high affinities depending on the divalent cations Zn2+ or Ni2+. COMP is a secreted glycoprotein that is important for growth plate organization and function. It is suggested to play a role in cell growth and development, and recent studies have revealed the possible mechanism that it protects cells against death by elevating members of the IAP (inhibitor of apoptosis protein) family of survival proteins. Mutations in COMP cause two skeletal dysplasias, pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (EDM1), and up-regulated expression of COMP are observed in rheumatoid arthritis and certain carcinomas.
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