目录号 | 产品详情 | 靶点 | |
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T21512 | MMP | ||
MMP-2/MMP-9-IN-1 是一种有效的、具有高选择性和可口服的 IV 型胶原酶 (MMP-9和MMP-2) 抑制剂,对 MMP-9 和 MMP-2具有抑制作用, IC50分别为 0.24 和 0.3 1μM。MMP-2/MMP-9-IN-1 在肿瘤生长和转移的动物模型中展现出口服活性,可用于研究癌症。 | |||
T8310 | MMP | ||
MMP-9-IN-1 是特异性的基质金属蛋白酶-9 抑制剂,选择性靶向 MMP-9 的血红素域,对其他 MMP 无影响。 | |||
T77617 | MMP | ||
MMP-9-IN-6 是一种 MMP-9 抑制剂,其 IC50 值为50 μM, 具有较好的抗溃疡功效。MMP-9-IN-6 具有潜在的抗肿瘤活性,可用于研究组织重塑、伤口修复和动脉粥样硬化。 | |||
T36712 | MMP | ||
BPHA (MMP-2/MMP-9 Inhibitor II) 是一种有效的、具有选择性和口服活性的抑制剂,对MMP-2、MMP-9 和 MMP-14 具有抑制作用,IC50 分别为 12 nM、16 nM 和 17 nM。BPHA 不抑制 MMP-1、-3 和 -7 (IC50 分别为 974、>1000 和 795 nM)。BPHA 具有抗血管生成和抗肿瘤活性。 | |||
T37726 | |||
MMP-9 inhibitor I is an inhibitor of matrix metalloproteinase-9 (MMP-9) that is selective over MMP-1 and MMP-13 (IC50s = 5, 1,050, and 113 nM, respectively). It also decreases the activity of TNF-α converting enzyme (TACE) in a dose-dependent manner (IC50 = 0.54 μM). MMP-9 inhibitor I decreases TNF-α secretion stimulated by LPS in BV-2 microglial cells when used at concentrations of 50 and 100 μM. | |||
T37172 | |||
MMP-9/MMP-13 Inhibitor I 是 MMP-9 和 MMP-13 双重抑制剂,IC50 均为 0.9 nM。MMP-9/MMP-13 Inhibitor I 对 MMP-9/MMP-13 的选择性是其他 MMP 的 20 倍以上。 | |||
T2009 | MMP | ||
SB-3CT 是一种可透过血脑屏障的、竞争性的金属蛋白酶MMP-2和MMP-9抑制剂,Ki 分别为 13.9 nM、600 nM。他对明胶酶具有高选择性。它具有神经保护和抗癌作用。 | |||
T72069 | |||
MMP-9-IN-7抑制前基质金属蛋白酶活化,可用于预防、治疗或改善 MMP9和/或 MMP13介导的综合征。 | |||
T22115 | NF-κB | ||
NF-κB Activation Inhibitor III 是一种NF-kB 抑制剂,抑制 TNF-α 诱导的MMP-9上调,靶向抑制下游的MAPK p38,可用于靶向 TNF-α 介导的肿瘤侵袭和转移的化疗研究。 | |||
TP1015 | Others | ||
NFAT Inhibitor (VIVIT peptide) 是NFAT 的细胞渗透性肽抑制剂,能够选择性抑制钙调磷酸酶介导的NFAT 脱磷酸作用。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-01248 | MMP-9 Protein, Human, Recombinant | Human | HEK293 | ||
Matrix metalloproteinases (MMPs) are neutral proteinases that are involved in the breakdown and remodeling of the extracellular matrix (ECM) under a variety of physiological and pathological conditions, such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. MMP9, also known as 92-kDa gelatinase B/type IV collagenase, is secreted from neutrophils, macrophages, and some transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. It plays an important role in tissue remodeling in normal and pathological inflammatory processes. MMP-9 is a major secretion product of macrophages and a component of cytoplasmic granules of neutrophils and is particularly important in the pathogenesis of inflammatory, infectious, and neoplastic diseases in many organs including the lung. This enzyme is also secreted by lymphocytes and stromal cells upon stimulation by inflammatory cytokines, or upon delivery of bi-directional activation signals following integrin-mediated cell-cell or cell-extracellular matrix (ECM) contacts. Since the integrity of the tissue architecture is closely dependent on the delicate balance between MMPs and their inhibitors, excessive production of MMP-9 is linked to tissue damage and degenerative inflammatory disorders. As a consequence, regulation of gene transcription and tissue-specific expression of MMP-9 in normal and diseased states are being actively investigated to pave the way for new therapeutic targets. Besides, the dramatic overexpression of MMP-9 in cancer and various inflammatory conditions points to the molecular mechanisms controlling its expression as a potential target for eventual rational therapeutic intervention.
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TMPY-01919 | MMP-9 Protein, Mouse, Recombinant | Mouse | HEK293 | ||
Matrix metalloproteinases (MMPs) are neutral proteinases that are involved in the breakdown and remodeling of the extracellular matrix (ECM) under a variety of physiological and pathological conditions, such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. MMP9, also known as 92-kDa gelatinase B/type IV collagenase, is secreted from neutrophils, macrophages, and some transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. It plays an important role in tissue remodeling in normal and pathological inflammatory processes. MMP-9 is a major secretion product of macrophages and a component of cytoplasmic granules of neutrophils and is particularly important in the pathogenesis of inflammatory, infectious, and neoplastic diseases in many organs including the lung. This enzyme is also secreted by lymphocytes and stromal cells upon stimulation by inflammatory cytokines, or upon delivery of bi-directional activation signals following integrin-mediated cell-cell or cell-extracellular matrix (ECM) contacts. Since the integrity of the tissue architecture is closely dependent on the delicate balance between MMPs and their inhibitors, excessive production of MMP-9 is linked to tissue damage and degenerative inflammatory disorders. As a consequence, regulation of gene transcription and tissue-specific expression of MMP-9 in normal and diseased states are being actively investigated to pave the way for new therapeutic targets. Besides, the dramatic overexpression of MMP-9 in cancer and various inflammatory conditions points to the molecular mechanisms controlling its expression as a potential target for eventual rational therapeutic intervention.
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TMPY-00888 | MMP-9 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Matrix metalloproteinases (MMPs) are neutral proteinases that are involved in the breakdown and remodeling of the extracellular matrix (ECM) under a variety of physiological and pathological conditions, such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. MMP9, also known as 92-kDa gelatinase B/type IV collagenase, is secreted from neutrophils, macrophages, and some transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. It plays an important role in tissue remodeling in normal and pathological inflammatory processes. MMP-9 is a major secretion product of macrophages and a component of cytoplasmic granules of neutrophils and is particularly important in the pathogenesis of inflammatory, infectious, and neoplastic diseases in many organs including the lung. This enzyme is also secreted by lymphocytes and stromal cells upon stimulation by inflammatory cytokines, or upon delivery of bi-directional activation signals following integrin-mediated cell-cell or cell-extracellular matrix (ECM) contacts. Since the integrity of the tissue architecture is closely dependent on the delicate balance between MMPs and their inhibitors, excessive production of MMP-9 is linked to tissue damage and degenerative inflammatory disorders. As a consequence, regulation of gene transcription and tissue-specific expression of MMP-9 in normal and diseased states are being actively investigated to pave the way for new therapeutic targets. Besides, the dramatic overexpression of MMP-9 in cancer and various inflammatory conditions points to the molecular mechanisms controlling its expression as a potential target for eventual rational therapeutic intervention.
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TMPK-00503 | MMP-9 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Matrix metalloproteinase 9 (MMP9) contributes to this process and deficiencies in the MMP9 lead to impaired healing. Inappropriate expression of MMP9 also contributes to impaired re-epithelialization. Previously we demonstrated that FOXO1 was activated in wound healing but to higher levels in diabetic wounds. To address mechanisms of impaired re-epithelialization we examined MMP9 expression in vivo in full thickness dermal scalp wounds created in experimental K14.
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TMPK-00367 | MMP-9 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Matrix metalloproteinase 9 (MMP9) contributes to this process and deficiencies in the MMP9 lead to impaired healing. Inappropriate expression of MMP9 also contributes to impaired re-epithelialization. Previously we demonstrated that FOXO1 was activated in wound healing but to higher levels in diabetic wounds. To address mechanisms of impaired re-epithelialization we examined MMP9 expression in vivo in full thickness dermal scalp wounds created in experimental K14.
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TMPK-00368 | MMP-9 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Matrix metalloproteinase 9 (MMP9) contributes to this process and deficiencies in the MMP9 lead to impaired healing. Inappropriate expression of MMP9 also contributes to impaired re-epithelialization. Previously we demonstrated that FOXO1 was activated in wound healing but to higher levels in diabetic wounds. To address mechanisms of impaired re-epithelialization we examined MMP9 expression in vivo in full thickness dermal scalp wounds created in experimental K14.
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TMPJ-00957 | MMP-9 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain.
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TMPY-02054 | MMP-9 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Matrix metalloproteinases (MMPs) are neutral proteinases that are involved in the breakdown and remodeling of the extracellular matrix (ECM) under a variety of physiological and pathological conditions, such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. MMP9, also known as 92-kDa gelatinase B/type IV collagenase, is secreted from neutrophils, macrophages, and some transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. It plays an important role in tissue remodeling in normal and pathological inflammatory processes. MMP-9 is a major secretion product of macrophages and a component of cytoplasmic granules of neutrophils and is particularly important in the pathogenesis of inflammatory, infectious, and neoplastic diseases in many organs including the lung. This enzyme is also secreted by lymphocytes and stromal cells upon stimulation by inflammatory cytokines, or upon delivery of bi-directional activation signals following integrin-mediated cell-cell or cell-extracellular matrix (ECM) contacts. Since the integrity of the tissue architecture is closely dependent on the delicate balance between MMPs and their inhibitors, excessive production of MMP-9 is linked to tissue damage and degenerative inflammatory disorders. As a consequence, regulation of gene transcription and tissue-specific expression of MMP-9 in normal and diseased states are being actively investigated to pave the way for new therapeutic targets. Besides, the dramatic overexpression of MMP-9 in cancer and various inflammatory conditions points to the molecular mechanisms controlling its expression as a potential target for eventual rational therapeutic intervention.
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TMPY-01107 | TIMP-1 Protein, Human, Recombinant | Human | HEK293 | ||
TIMP metallopeptidase inhibitor 1, also known as TIMP-1/TIMP1, Collagenase inhibitor 16C8 fibroblast Erythroid-potentiating activity, TPA-S1TPA-induced proteinTissue inhibitor of metalloproteinases 1, is a natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. TIMP-1/TIMP1 is found in fetal and adult tissues. Highest levels are found in bone, lung, ovary and uterus. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. In addition to its inhibitory role against most of the known MMPs, the protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this protein encoding gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This encoding gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 is Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16.
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TMPJ-01289 | TIMP-4 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Metalloproteinase inhibitor 4 is an enzyme that in humans is encoded by the TIMP4 gene, belongs to the protease inhibitor I35 (TIMP) family. The protein complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP-9.
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TMPH-01665 | TIMP3 Protein, Human, Recombinant (His) | Human | E. coli | ||
Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.
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TMPJ-00447 | MMP-3 Protein, Human, Recombinant (His) | Human | Human Cells | ||
MMP3 is a member of the matrix metalloproteinase (MMP) family whose members are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, tissue remodeling, and disease processes including arthritis and metastasis. The MMP-3 enzyme degrades collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. In addition, MMP-3 can also activate other MMPs such as MMP-1, MMP-7, and MMP-9, rendering MMP-3 crucial in connective tissue remodeling.[3] The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation.
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TMPK-01286 | MMP-8 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Alteration of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) expression has been studied for various cardiac diseases, including dilated cardiomyopathy (DCM), with the significance of surrogate markers of extracellular matrix (ECM) remodeling. MMP-8 was identified only in myocardiocytes, while MMP-9 and TIMP-2 were present in both myocardiocytes and stroma, but with different intensity. The increasing intensity of MMP-8 and TIMP-2 immunoreactions was significantly associated with low HCS.
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TMPJ-00865 | VEGF121 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Human VEGF121, also known as Vascular endothelial growth factor A, VEGFA, Vascular permeability factor, VPF and VEGF, is a homodimeric, heparin-binding glycoprotein which belongs to the platelet-derived growth factor (PDGF)/vascular endothelial growth factor (VEGF) family. VEGF-A is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis, permeabilization of blood vessels and endothelial cell growth, increasing microvascular permeability, promoting cell migration and inhibiting apoptosis. Alternatively spliced transcript variants of VEGF-A encod either secreted or cell-associated isoforms. The lymphangiogenesis may be promoted by upregulation of VEGF121, which may in turn act in part via induction of VEGF-C. It binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth.
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TMPJ-00082 | NGAL/Lipocalin-2 Protein, Mouse, Recombinant (hFc) | Mouse | Human Cells | ||
Lipocalin-2, also known as Neutrophil Gelatinase-Associated Lipocalin (NGAL), is a secretory protein of the lipocalin superfamily. Lipocalin-2 contains a signal peptide that enables it to be secreted and form complexes with matrix metalloproteinase-9 (MMP-9) through disulfide bonds. Similar to other lipocalin family members, Lipocalin-2 is involved in diverse cellular processes, including the transport of small hydrophobic molecules, protection of MMP-9 from proteolytic degradation, and cell signaling. Furthermore, Lipocalin-2 can tightly bind to bacterial siderophore through a cell surface receptor, possibly serving as a potent bacteriostatic agent by sequestering iron, regulating innate immunity and protecting kidney epithelial cells from ischemia–reperfusion injury. This protein is mainly expressed in neutrophils and in lower levels in the kidney, prostate, and epithelia of the respiratory and alimentary tracts.Recent evidence also suggests its role as a biomarker for renal injury and inflammation.
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TMPY-01485 | TIMP-1 Protein, Mouse, Recombinant | Mouse | HEK293 | ||
TIMP metallopeptidase inhibitor 1, also known as TIMP-1/TIMP1, Collagenase inhibitor 16C8 fibroblast Erythroid-potentiating activity, TPA-S1TPA-induced proteinTissue inhibitor of metalloproteinases 1, is a natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. TIMP-1/TIMP1 is found in fetal and adult tissues. Highest levels are found in bone, lung, ovary and uterus. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. In addition to its inhibitory role against most of the known MMPs, the protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this protein encoding gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This encoding gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 is Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16.
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TMPY-02912 | TIMP-1 Protein, Rat, Recombinant | Rat | HEK293 | ||
TIMP metallopeptidase inhibitor 1, also known as TIMP-1/TIMP1, Collagenase inhibitor 16C8 fibroblast Erythroid-potentiating activity, TPA-S1TPA-induced proteinTissue inhibitor of metalloproteinases 1, is a natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. TIMP-1/TIMP1 is found in fetal and adult tissues. Highest levels are found in bone, lung, ovary and uterus. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. In addition to its inhibitory role against most of the known MMPs, the protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this protein encoding gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This encoding gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 is Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16.
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TMPY-00154 | TIMP-1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
TIMP metallopeptidase inhibitor 1, also known as TIMP-1/TIMP1, Collagenase inhibitor 16C8 fibroblast Erythroid-potentiating activity, TPA-S1TPA-induced proteinTissue inhibitor of metalloproteinases 1, is a natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. TIMP-1/TIMP1 is found in fetal and adult tissues. Highest levels are found in bone, lung, ovary and uterus. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. In addition to its inhibitory role against most of the known MMPs, the protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this protein encoding gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This encoding gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 is Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16.
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TMPY-00932 | TIMP-1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
TIMP metallopeptidase inhibitor 1, also known as TIMP-1/TIMP1, Collagenase inhibitor 16C8 fibroblast Erythroid-potentiating activity, TPA-S1TPA-induced proteinTissue inhibitor of metalloproteinases 1, is a natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. TIMP-1/TIMP1 is found in fetal and adult tissues. Highest levels are found in bone, lung, ovary and uterus. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. In addition to its inhibitory role against most of the known MMPs, the protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this protein encoding gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This encoding gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 is Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16.
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TMPY-03698 | VEGF121b Protein, Human, Recombinant | Human | HEK293 | ||
Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF) and VEGF-A, is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult. It is a member of the platelet-derived growth factor (PDGF)/vascular endothelial growth factor (VEGF) family and often exists as a disulfide-linked homodimer. VEGF-A protein is a glycosylated mitogen that specifically acts on endothelial cells and has various effects, including mediating increased vascular permeability, inducing angiogenesis, vasculogenesis and endothelial cell growth, promoting cell migration, inhibiting apoptosis and tumor growth. VEGF-A protein is also a vasodilator that increases microvascular permeability, thus it was originally referred to as vascular permeability factor.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-00005 | YAP1 Protein, Human, Recombinant (Isoform 9, His) | Human | Yeast | ||
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TMPY-00486 | ALK-7 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
ALK-7, also known as ALK7 and ACVR1C, belongs to the ALK family. It is a type I receptor for the TGFB family of signaling molecules. TGF-β is the prototype of a protein superfamily which, in humans, contains at least 35 members, including activins, inhibins, bone morphogenetic proteins, growth/differentiation factors, and Müllerian inhibiting substance. ALK-7 is a serine-threonine kinase that can cause the activation of one of the SMAD signal transducers, SMAD2. ALK-7 has a ligand known as Nodal. Nodal stimulates the secretion of TIMP-1 and inhibits matrix metalloproteinases MMP-2 and MMP-9 activity. The overexpression of Nodal or constitutively active ALK-7 decreases cell migration and invasion, whereas knock-down of Nodal and ALK-7 has the opposite effects.
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TMPY-03187 | ALK-7 Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
ALK-7, also known as ALK7 and ACVR1C, belongs to the ALK family. It is a type I receptor for the TGFB family of signaling molecules. TGF-β is the prototype of a protein superfamily which, in humans, contains at least 35 members, including activins, inhibins, bone morphogenetic proteins, growth/differentiation factors, and Müllerian inhibiting substance. ALK-7 is a serine-threonine kinase that can cause the activation of one of the SMAD signal transducers, SMAD2. ALK-7 has a ligand known as Nodal. Nodal stimulates the secretion of TIMP-1 and inhibits matrix metalloproteinases MMP-2 and MMP-9 activity. The overexpression of Nodal or constitutively active ALK-7 decreases cell migration and invasion, whereas knock-down of Nodal and ALK-7 has the opposite effects.
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TMPY-00886 | MMP-1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
MMP1, also known as MMP-1, contains 4 hemopexin-like domains and is a member of the matrix metalloproteinase (MMP) family. Matrix metalloproteases, also called matrixins, are zinc-dependent endopeptidases that are the major proteases involved in ECM degradation. MMPs are capable of degrading a wide range of extracellular molecules and some bioactive molecules. MMP activity is regulated by two major endogenous inhibitors: alpha2-macroglobulin and tissue inhibitors of metalloproteases (TIMPs). MMPs play a central role in cell proliferation, migration, differentiation, angiogenesis, apoptosis, and host defenses. Dysregulation of MMPs has been implicated in many diseases including arthritis, chronic ulcers, encephalomyelitis, and cancer. Tumour metastasis is a multistep process involving the dissemination of tumor cells from the primary tumor to secondary at a distant organ or tissue. One of the first steps in metastasis is the degradation of the basement membrane, a process in which MMPs have been implicated. MMPs are secreted by tumor cells themselves or by surrounding stromal cells stimulated by the nearby tumor. Numerous studies have linked altered MMP expression in different human cancers with poor disease prognosis. MMP-1, -2, -3, -7, -9, -13 and -14 all have elevated expression in primary tumors and/or metastases. MMP-1 cleaves collagens of types I, II, and III at one site in the helical domain. It also cleaves collagens of types VII and X. In case of HIV infection, MMP1 interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.
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TMPJ-00948 | Endostatin Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Endostatin, an endogenous non‑glycosylated inhibitor of endothelial cell proliferation and angiogenesis. It is produced and/or trimmed by metalloproteinases such as MMP‑2 and MMP‑9, and cathepsins S, B and L. The N‑terminal ~27 aa of Endostatin appear to contain the majority of its activity. This region contains zinc binding sites that are thought to be critical for its anti‑endothelial and anti‑tumor effects, as well as multiple cleavage sites that, when used, can modify its activity. Mouse Endostatin shares 96% aa sequence identity with rat and 85‑87% with human, bovine and equine Endostatin. It is predominantly expressed in liver, kidney, lung, skeletal muscle and testis. Endostatin inhibits endothelial cell growth by inducing cell cycle arrest in G1 phase and initiating apoptosis. It is also thought to down‑regulate angiogenesis by blocking VEGF‑induced endothelial cell migration. Endostatin may also be involved with down‑regulation of angiogenesis after establishment of placental circulation in the pregnant uterus.
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TMPY-02404 | ADAM9 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
ADAM9 (A disintegrin and metallopeptidase domain 9, MDC9, meltrin gamma), is a type 1 transmembrane protein that has been associated with cancer development and metastases. ADAM9 is consistently overexpressed in various human cancers, and plays a role in tumorigenesis in mouse models. ADAM9 cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as EGF, FGFR2iiib, Tie-2, Flk-1, EphB4, CD40, VCAM-1, and VE-cadherin, and could represent a potential therapeutic target in tumors where it is highly expressed. ADAM9 belongs to a family of transmembrane, disintegrin-containing metalloproteinases involved in protein ectodomain shedding and cell-cell and cell-matrix interactions. ADAM-9 adhesive domain plays a role in regulating the motility of cells by interaction with beta1 integrins and modulates MMP synthesis.
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TMPJ-01060 | CXCL6 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Chemokine (C-X-C-Motif) Ligand 6 (CXCL6) is a small cytokine belonging to the CXC chemokine family. It is a potent neutrophil chemotactic and activating factor and it exhibits extensive similarity to other CXC chemokines such as IL-8 and ENA-78. CXCL6 can promote the release of MMP-9 from granulocytes indicating its potential role as an inflammatory mediator. It functionally uses both of the IL-8/CXCL8 receptors to chemoattract neutrophils but that is structurally most related to epithelial cell-derived neutrophil attractant-78 (ENA-78)/CXCL5. The human CXCL6 gene has been cloned and is physically mapped to the CXC chemokine locus on chromosome 4. Mature human CXCL6 is a 75 amino acid (aa) protein with a predicted molecular weight of approximately 8 kDa. Human CXCL6 shares 60% and 67% aa identity with mouse and bovine CXCL6, respectively.
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TMPK-00825 | VEGF121 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Vascular endothelial growth factor (VEGF or VEGF-A), also known as vascular permeability factor (VPF), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult. VEGF165 appears to be the most abundant and potent isoform, followed by VEGF121 and VEGF189.
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TMPK-00826 | VEGF121 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 | ||
Vascular endothelial growth factor (VEGF or VEGF-A), also known as vascular permeability factor (VPF), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult. VEGF165 appears to be the most abundant and potent isoform, followed by VEGF121 and VEGF189.
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TMPY-05268 | Neurofascin Protein, Human, Recombinant (hFc), Biotinylated | Human | HEK293 | ||
NFASC (Neurofascin, also known as NRCAML, NEDCPMD, and NF) is a Protein Coding gene. 13 alternatively spliced human isoforms have been reported. NFASC belongs to the immunoglobulin superfamily, L1/neurofascin/NgCAM family. It contains 5 fibronectin type-III domains and 6 Ig-like C2-type (immunoglobulin-like) domains. The protein functions in neurite outgrowth, neurite fasciculation, and organization of the axon initial segment (AIS) and nodes of Ranvier on axons during early development. NFASC links the AIS extracellular matrix to the intracellular cytoskeleton. It is broadly expressed in the brain, kidney, and other tissues. Diseases associated with NFASC include Neurodevelopmental Disorder With Central And Peripheral Motor Dysfunction and Demyelinating Polyneuropathy.
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