目录号 | 产品详情 | 靶点 | |
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TP1717 | |||
CEF1, Influenza Matrix Protein M1 (58-66) is an epitope derived from the matrix protein of the influenza A virus.GILGFVFTL is a HLA-A2-restricted epitope from influenza matrix M1 protein. | |||
T38687 | |||
Influenza Matrix Protein (61-72) is a peptide derived from the matrix protein of influenza viruses and encompasses amino acids 61-72. This specific epitope, Influenza Matrix Protein (61-72), has the ability to elicit a CD4+ T-cell response. | |||
TP2184 | Others | ||
matrix protein (3-15) [Zaire ebolavirus] is a peptide of the structural proteins linking the viral envelope with the zaire ebolavirus core. Ebola virus (EBOV) is a member of the family Filoviridae in the order Mononegavirales. It is the causative agent of | |||
T69665 | |||
Zelasudil 是一种 Rho 相关 (ROCK) 激酶 抑制剂。Zelasudil 具有 ROCK2结合亲和力。 | |||
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。 | |||
T5361 | MMP | ||
T-26c 是高效的、选择性的基质金属蛋白酶-13 抑制剂,IC50=6.75 pM。 | |||
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。 | |||
T14978 | MMP | ||
CL-82198 是 MMP-13选择性抑制剂。它能够与 MMP-13 的整个 S1' 口袋结合,这是其对 MMP-13 选择性和对其他 MMP 缺乏抑制活性的基础。它可用于研究骨关节炎。 | |||
T4783 | MMP | ||
JNJ0966 是高选择性 MMP-9酶原抑制剂,其 IC50=440 nM。 | |||
T14322 | MMP | ||
ARP-100 (MMP-2 Inhibitor III) 是选择性基质金属蛋白酶MMP-2抑制剂 (IC50=12 nM)。它对 MMP-1 (>50 μM),MMP-3 (4.5 μM),MMP-7 (>50 μM) 和MMP-9 (0.2 μM) 的抑制活性较小。它与 MMP-2 的 S1'口袋相互作用,并在体外对基质胶的侵袭模型中显示抗侵袭特性。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-02869 | MMP-12 Protein, Human, Recombinant (catalytic domain) | Human | E. coli | ||
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Macrophage Metalloelastase, also known as Matrix metalloproteinase-12, Macrophage elastase, MMP12, and MMP-12, is a secreted protein that belongs to the peptidase M1A family. MMP12 is a macrophage-secreted elastase that is highly induced in the liver and lung in response to S. mansoni eggs and contains four hemopexin-like domains. MMP12 is a proteolytic enzyme responsible for the cleavage of plasminogen to angiotensin, which has an angiostatic effect. It may be involved in tissue injury and remodeling and has significant elastolytic activity. It may be related to prognosis in breast cancer patients. MMP12 promotes fibrosis by limiting the expression of specific ECM-degrading MMPs. Like MMP12, MMP13 expression is highly dependent on IL-13 and type I I-IL-4 receptor signaling. MMP12 is a potent proinflammatory and oncogenic molecule. MMP12 up-regulation plays a critical role in emphysema to lung cancer transition that is facilitated by inflammation.
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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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TMPY-01884 | MMP-8 Protein, Human, Recombinant | Human | HEK293 | ||
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Neutrophil collagenase, also known as Matrix metalloproteinase-8, MMP-8, and CLG1, is a member of the peptidase M1A family. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 in the tumor may have a protective effect against lymph node metastasis. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 participates in wound repair by contributing to the resolution of inflammation and open the possibility to develop new strategies for treating wound healing defects.
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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-01477 | MMP-2 Protein, Human, Recombinant | Human | HEK293 | ||
Matrix Metalloproteinase-2 (MMP-2) is an enzyme that degrades components of the extracellular matrix and thus plays a pivotal role in cell migration during physiological and pathological processes. MMP-2 expression is dependent on extracellular matrix metalloproteinase inducer (EMMPRIN), Her2/neu, growth factors, cytokines, and hormones. Pro-MMP-2 activation needs MT1-MMP and TIMP-2 contribution. MMP-2 is changed in distribution and increased in amount in the ventral cochlear nucleus after unilateral cochlear ablation. A low level of MMP-2 is linked to a favorable prognosis in patients with a hormone receptor-negative tumor, usually associated with high risk. As a zymogen requiring proteolytic activation for catalytic activity, MMP-2 has been implicated broadly in the invasion and metastasis of many cancer model systems, including human breast cancer (HBC). Blocking MMP-2 secretion and activation during breast carcinoma development may decrease metastasis. The detection of active MMP-2 alone or the rate of pro-MMP-2 and active MMP-2 is considered a very sensitive indicator of cancer metastasis. Modulation of MMP-2 expression and activation through specific inhibitors and activators may thus provide a new mechanism for breast cancer treatment.
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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-00333 | ECM1 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Extracellular matrix protein 1 (ECM1) is a secreted glycoprotein and playing a pivotal role in endochondral bone formation, angiogenesis, and tumour biology. Three splice variants have been identified: ECM1a (540 aa) is most widely expressed, with highest expression in the placenta and heart; ECM1b (415 aa) is differentiation-dependent expressed and found only in tonsil and associated with suprabasal keratinocytes; ECM1c (559 aa) accounts for approximately 15% of skin ECM1. Although ECM1 is not tumor specific, is significantly elevated in many malignant epithelial tumors and is suggested as a possible trigger for angiogenesis, tumor progression and malignancies. It also has been shown to regulate endochondral bone formation, skeletal development and tissue remodeling.
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TMPY-04100 | MMP-26 Protein, Human, Recombinant | Human | E. coli | ||
MMP26 (Matrix Metallopeptidase 26) is a Protein Coding gene. MMP26 is a member of matrix metalloproteinases (MMPs) and has been reported to be highly expressed in many cancers. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain. It may hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin, and alpha-1 proteinase inhibitor, and is also able to activate progelatinase B. MMP26 is a target gene of miR-125b, and the expression profile of MMP26 showed an inverse relationship with miR-125b in vivo and in vitro. The overexpression of MMP26 in SW1353 cells increased cell invasiveness, while inhibition of MMP26 decreased cell invasiveness.
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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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TMPY-01844 | MMP-8 Protein, Mouse, Recombinant | Mouse | HEK293 | ||
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Neutrophil collagenase, also known as Matrix metalloproteinase-8, MMP-8, and CLG1, is a member of the peptidase M1A family. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 in the tumor may have a protective effect against lymph node metastasis. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 participates in wound repair by contributing to the resolution of inflammation and open the possibility to develop new strategies for treating wound healing defects.
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TMPY-00520 | MMP-8 Protein, Mouse, Recombinant (His) | Mouse | CHO | ||
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Neutrophil collagenase, also known as Matrix metalloproteinase-8, MMP-8, and CLG1, is a member of the peptidase M1A family. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 in the tumor may have a protective effect against lymph node metastasis. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 participates in wound repair by contributing to the resolution of inflammation and open the possibility to develop new strategies for treating wound healing defects.
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TMPY-01908 | ECM1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Extracellular matrix protein 1 (ECM1) is a secreted glycoprotein and playing a pivotal role in endochondral bone formation, angiogenesis, and tumour biology. Three splice variants have been identified: ECM1a (540 aa) is most widely expressed, with highest expression in the placenta and heart; ECM1b (415 aa) is differentiation-dependent expressed and found only in tonsil and associated with suprabasal keratinocytes; ECM1c (559 aa) accounts for approximately 15% of skin ECM1. Although ECM1 is not tumor specific, is significantly elevated in many malignant epithelial tumors and is suggested as a possible trigger for angiogenesis, tumor progression and malignancies. It also has been shown to regulate endochondral bone formation, skeletal development and tissue remodeling.
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TMPY-00065 | Ebola virus EBOV (subtype Bundibugyo, strain Uganda 2007) VP40/Matrix protein VP40 Protein (His) | EBOV | E. coli | ||
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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-06314 | MMP-10 Protein, Human, Recombinant (HEK293, His) | Human | HEK293 | ||
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TMPY-02290 | MMP-2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Matrix Metalloproteinase-2 (MMP-2) is an enzyme that degrades components of the extracellular matrix and thus plays a pivotal role in cell migration during physiological and pathological processes. MMP-2 expression is dependent on extracellular matrix metalloproteinase inducer (EMMPRIN), Her2/neu, growth factors, cytokines, and hormones. Pro-MMP-2 activation needs MT1-MMP and TIMP-2 contribution. MMP-2 is changed in distribution and increased in amount in the ventral cochlear nucleus after unilateral cochlear ablation. A low level of MMP-2 is linked to a favorable prognosis in patients with a hormone receptor-negative tumor, usually associated with high risk. As a zymogen requiring proteolytic activation for catalytic activity, MMP-2 has been implicated broadly in the invasion and metastasis of many cancer model systems, including human breast cancer (HBC). Blocking MMP-2 secretion and activation during breast carcinoma development may decrease metastasis. The detection of active MMP-2 alone or the rate of pro-MMP-2 and active MMP-2 is considered a very sensitive indicator of cancer metastasis. Modulation of MMP-2 expression and activation through specific inhibitors and activators may thus provide a new mechanism for breast cancer treatment.
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TMPY-02286 | Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Matrix protein 1/M1 Protein (His) | H1N1 | E. coli | ||
The Influenza virus matrix protein 1 (M1) is a matrix protein of the influenza virus. M1 protein has been shown to play a crucial role in virus replication, assembly, and budding. It forms a coat inside the viral envelope. This is a bifunctional membrane/RNA-binding protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. M1 consists of two domains connected by a linker sequence. The N-terminal domain has a multi-helical structure. The C-terminal domain also contains an alpha-helical structure. The M1 protein is the most abundant structural protein in influenza A virus particles. M1 protein of the influenza A virus plays multiple roles in virion assembly and infection. M1 protein was a candidate antigen for a broad-spectrum influenza virus vaccine and the adjuvant chitosan significantly improved the efficacy of the M1 vaccine.
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TMPY-02010 | DMP1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Dentin matrix acidic phosphoprotein (DMP1) is an extracellular matrix protein and a member of the small integrin binding ligand N-linked glycoprotein family. This protein, which is critical for proper mineralization of bone and dentin, is present in diverse cells of bone and tooth tissues. DMP1 contains a large number of acidic domains, multiple phosphorylation sites, a functional arg-gly-asp cell attachment sequence, and a DNA binding domain. In undifferentiated osteoblasts it is primarily a nuclear protein that regulates the expression of osteoblast-specific genes. During osteoblast maturation, DMP1 becomes phosphorylated and is exported to the extracellular matrix, where it orchestrates mineralized matrix formation. Mutations in DMP1 are known to cause autosomal recessive hypophosphatemia, a disease that manifests as rickets and osteomalacia. DMP1 may have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite.
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TMPY-01377 | MMP-8 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Neutrophil collagenase, also known as Matrix metalloproteinase-8, MMP-8, and CLG1, is a member of the peptidase M1A family. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 in the tumor may have a protective effect against lymph node metastasis. MMP-8 may affect the metastatic behavior of breast cancer cells through protection against lymph node metastasis, underlining the importance of anti-target identification in drug development. MMP-8 participates in wound repair by contributing to the resolution of inflammation and open the possibility to develop new strategies for treating wound healing defects.
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TMPJ-01085 | DPT Protein, Human, Recombinant (hFc & His) | Human | Human Cells | ||
Dermatopontin, also known as Tyrosine-rich acidic matrix protein, TRAMP and DPT, is a secreted protein which belongs to the dermatopontin family. DPT is expressed in various tissues, such as fibroblasts, heart, skeletal muscle, brain and pancreas. It seems to mediate adhesion by cell surface integrin binding. DPT may serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment. DPT can enhance TGFB1 activity through interaction with decorin. In addition, DPT accelerates collagen fibril formation, stabilizes collagen fibrils against low-temperature dissociation and inhibits cell proliferation.
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TMPH-03693 | VSIV (strain Glasgow) Matrix Protein (His) | VSIV | E. coli | ||
VSIV (strain Glasgow) Matrix Protein (His) is expressed in E. coli.
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TMPJ-01245 | UCMA Protein, Human, Recombinant | Human | E. coli | ||
C10orf49 is a secreted protein which encoded by the UCMA gene. It is a member of the UCMA family. C10orf49 is predominantly expressed in resting chondrocytes. It may be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
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TMPJ-00942 | MMP-12 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Matrix metalloproteinase-12(MMP12) is a secreted protein.It contains 4 hemopexin repeats and belongs to the peptidase M10A family. MMP12 may be involved in tissue injury and remodeling and have significant elastolytic activity. It can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
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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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TMPH-01316 | ECM1 Protein, Human, Recombinant (GST & His & Myc) | Human | E. coli | ||
Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity.
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TMPH-03692 | VSIV (strain San Juan) Matrix Protein (His & Myc) | VSIV | E. coli | ||
VSIV (strain San Juan) Matrix Protein (His & Myc) is expressed in E. coli.
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TMPJ-01369 | DPT Protein, Mouse, Recombinant (hFc) | Mouse | Human Cells | ||
Dermatopontin is a widely expressed noncollagenous protein component of the extracellular matrix. It is a 22 kDa molecule that is tyrosine sulfated but not glycosylated. Dermatopontin is down regulated in fibrotic growths such as leiomyoma and scar tissue, inhibits cell proliferation, accelerates collagen fibril formation, and stabilizes collagen fibrils against low-temperature dissociation, Dermatopontin deficient mice exhibit altered collagen matrix deposition and organization. Dermatopontin seems to mediate adhesion by cell surface integrin binding, may serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment, and enhances TGFB1 activity (By similarity). Dermatopontin promotes bone mineralization under the control of the vitamin D receptor and inhibits BMP-2 effects on osteoblast precursors.
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TMPH-03430 | ECM31 Protein, S. cerevisiae, Recombinant (His) | Saccharomyces cerevisiae | E. coli | ||
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TMPH-03694 | VSIV (strain Glasgow) Matrix Protein (His & Myc) | VSIV | Baculovirus | ||
VSIV (strain Glasgow) Matrix Protein (His & Myc) is expressed in Baculovirus.
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TMPY-02689 | MMP-3 Protein, Human, Recombinant | Human | E. coli | ||
Matrix metallopeptidase 3 (abbreviated as MMP3) is also known as stromelysin 1 and progelatinase. 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. As a secreted zinc-dependent endopeptidase, MMP3 exerts its functions mainly in the extracellular matrix. This protein is activated by two major endogenous inhibitors: alpha2-macroglobulin and tissue inhibitors of metalloproteases (TIMPs). MMP3 plays a central role in degrading collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. Also, MMP3 can active other MMPs such as MMP1, MMP7, and MMP9, rendering MMP3 crucial in connective tissue remodeling. Dysregulation of MMPs has been implicated in many diseases including arthritis, chronic ulcers, encephalomyelitis, and cancer. Synthetic or natural inhibitors of MMPs result in inhibition of metastasis, while up-regulation of MMPs led to enhanced cancer cell invasion.
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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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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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TMPH-01673 | Human metapneumovirus (strain CAN97-83) Matrix protein (His) | HMPV | Yeast | ||
Plays a crucial role in virus assembly into filaments and budding. Early in infection, localizes in the nucleus where it may inhibit host cell transcription. Later in infection, traffics to the cytoplasm through the action of host CRM1 to associate with inclusion bodies, the site of viral transcription and replication. During virus assembly and budding, acts as a bridge between the nucleocapsid and the lipid bilayer.
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TMPH-01672 | Human metapneumovirus (strain CAN97-83) Matrix protein (His & Myc) | HMPV | E. coli | ||
Plays a crucial role in virus assembly into filaments and budding. Early in infection, localizes in the nucleus where it may inhibit host cell transcription. Later in infection, traffics to the cytoplasm through the action of host CRM1 to associate with inclusion bodies, the site of viral transcription and replication. During virus assembly and budding, acts as a bridge between the nucleocapsid and the lipid bilayer.
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TMPH-03228 | Rabies virus (RABV) (strain SAD B19) Matrix Protein (His) | RABV | E. coli | ||
Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases.
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TMPH-03227 | Rabies virus (RABV) (strain PM1503/AVO1) Matrix Protein (His) | RABV | E. coli | ||
Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases.
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TMPH-03695 | VSIV (strain 98COE North America) Matrix Protein (His & Myc) | VSIV | E. coli | ||
VSIV (strain 98COE North America) Matrix Protein (His & Myc) is expressed in E. coli.
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TMPH-03226 | Rabies virus (RABV) (strain PM1503/AVO1) Matrix Protein (GST) | RABV | E. coli | ||
Plays a major role in assembly, budding and uncoating of virion after membrane fusion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication. Plays a major role in early induction of TRAIL-mediated apoptosis in infected neurons.
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TMPH-03225 | Rabies virus (RABV) (strain CVS-11) Matrix Protein (His & Myc) | RABV | E. coli | ||
Plays a major role in assembly, budding and uncoating of virion after membrane fusion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication. Plays a major role in early induction of TRAIL-mediated apoptosis in infected neurons.
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TMPJ-00362 | MMP-2 Protein, Human, Recombinant (His) | Human | Human Cells | ||
72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene.It belongs to the matrix metalloproteinase (MMP) family. Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. MMP-2 is ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, atherosclerotic plaque rupture, as well as degrading extracellular matrix proteins. MMP-2 can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. MMP-2 cleaves KISS at a Gly-|-Leu bond and appears to have a role in myocardial cell death pathways.
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TMPJ-00242 | PARVA Protein, Human, Recombinant (His) | Human | E. coli | ||
Alpha-Parvin (PARVA) is a member of the Parvin family. PARVA contains two CH (calponin-homology) domains. PARVA is widely expressed, with highest levels in heart, skeletal muscle, kidney and liver. PARVA interacts with integrin-linked protein kinase and probably with actin and the LD1 and LD4 motifs of PXN. PARVA may play a role in the regulation of cell adhesion and cytoskeleton organization. PARVA is also involved in ciliogenesis.
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TMPH-02382 | Lake Victoria marburgvirus (MARV) (strain Angola/2005) Matrix protein VP40 (His & SUMO) | MARV | E. coli | ||
Plays an essential role virus particle assembly and budding. Promotes virus assembly and budding by interacting with host proteins of the multivesicular body pathway. The interaction with host E3 ubiquitin ligase SMURF2 facilitates virus budding. The interaction with the nucleocapsid and the plasma membrane may also facilitate virus budding. Specific interactions with membrane-associated GP and VP24 during the budding process may also occur. May play a role in genome replication.
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TMPH-00998 | CD147 Protein, Human, Recombinant (aa 138-323, hFc) | Human | HEK293 | ||
CD147 Protein, Human, Recombinant (aa 138-323, hFc) is expressed in HEK293.
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TMPH-01071 | CD44 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion.
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TMPH-02347 | Influenza A H1N1 (strain A/USA:Phila/1935) Matrix protein 2 (His) | H1N1 | E. coli | ||
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.
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TMPH-02348 | Influenza A H1N1 (strain A/Puerto Rico/8/1934) Matrix protein 2 (His & Myc) | H1N1 | E. coli | ||
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.
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TMPY-00498 | Influenza A H3N2 (A/Aichi/2/1968) Matrix protein 1/M1 Protein (His) | H3N2 | E. coli | ||
The Influenza virus matrix protein 1 (M1) is a matrix protein of the influenza virus. M1 protein has been shown to play a crucial role in virus replication, assembly, and budding. It forms a coat inside the viral envelope. This is a bifunctional membrane/RNA-binding protein that mediates the encapsidation of RNA-nucleoprotein cores into the membrane envelope. M1 consists of two domains connected by a linker sequence. The N-terminal domain has a multi-helical structure. The C-terminal domain also contains an alpha-helical structure. The M1 protein is the most abundant structural protein in influenza A virus particles. M1 protein of the influenza A virus plays multiple roles in virion assembly and infection. M1 protein was a candidate antigen for a broad-spectrum influenza virus vaccine and the adjuvant chitosan significantly improved the efficacy of the M1 vaccine.
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TMPH-01072 | CD44 Protein, Human, Recombinant (Avi & mFc), Biotinylated | Human | HEK293 | ||
Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion.
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TMPH-02346 | Influenza A H1N1 (strain A/USA:Iowa/1943) Matrix protein 1 (His & Myc) | H1N1 | E. coli | ||
Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.; Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.
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