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Código de Artigo: (BOSSBS-4588R-CY3)
Fornecedor: Bioss
Descrição: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-1377R-A555)
Fornecedor: Bioss
Descrição: Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, 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. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-7928R-FITC)
Fornecedor: Bioss
Descrição: Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK (see MIM 601795), JNK (see MIM 601158), and p38 (see MIM 600289) with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-7928R-CY5.5)
Fornecedor: Bioss
Descrição: Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK (see MIM 601795), JNK (see MIM 601158), and p38 (see MIM 600289) with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-7928R-CY7)
Fornecedor: Bioss
Descrição: Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK (see MIM 601795), JNK (see MIM 601158), and p38 (see MIM 600289) with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-2959R-A680)
Fornecedor: Bioss
Descrição: Serotonin (5-hydroxytryptamine, 5-HT), a neurotransmitter, elicits a wide array of physiological effects by binding to several receptor subtypes, including the 5-HT2 family of seven-transmembrane-spanning, G-protein-coupled receptors, which activate phospholipase C and D signaling pathways. This gene encodes the 2C subtype of serotonin receptor and its mRNA is subject to multiple RNA editing events, where genomically encoded adenosine residues are converted to inosines. RNA editing is predicted to alter amino acids within the second intracellular loop of the 5-HT2C receptor and generate receptor isoforms that differ in their ability to interact with G proteins and the activation of phospholipase C and D signaling cascades, thus modulating serotonergic neurotransmission in the central nervous system. Studies in humans have reported abnormalities in patterns of 5-HT2C editing in depressed suicide victims.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-13281R-A488)
Fornecedor: Bioss
Descrição: The mammalian c-H-, c-K- and N-Ras proto-oncogenes encode ubiquitously expressed proteins (1,2). p21Ras can exist in either a physiologically quiescent GDP-binding state or a GTP-binding signal-emitting state (3). Oncogenic p21Ras proteins are trapped in the excited signal-emitting state because the mechanism normally employed to delimit their excitation period, hydrolysis of their bound GTP to GDP, is impaired as a result of specific mutations (3). Interaction of p21Ras with GTPase activating protein (GAP) can increase hydrolysis of p21Ras-bound GTP by as much as 1000-fold (4,5). The product of the neurofibromatosis type 1 gene (NF1) has also been shown to exhibit p21Ras GAP activity (6,7), and proteins that stimulate the GTPase activity of three other low molecular weight GTPases, including Rho, Rab 3A and Rap 1, have also been described (8,9).
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-1377R-A488)
Fornecedor: Bioss
Descrição: Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, 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. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-1377R-A647)
Fornecedor: Bioss
Descrição: Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodelling, 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. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-1377R)
Fornecedor: Bioss
Descrição: Matrix metalloproteinase 26 preprotein; gelatinase A; 70kD type IV collagenase; gelatinase neutrophil. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes as well as in disease processes. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP26 degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response.Proteins of the matrix metalloproteinase (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. MMP26, also known as Matrilysin 2, was first cloned from human fetal cells, and identified as an MMP most closely related to MMP7 (Matrilysin 1). The homology between MMP7 and MMP26 is low (only 38% identical), thus the functions are unlikely to be similar. Homology is much higher (48% identical) for the comparable region of MMP12, but MMP26 appears to have broader substrate specificity than does MMP12. MMP26, like MMP7, lacks the hemopexin domain common to the other MMPs, but contains a Propeptide domain, cysteine switch activation site, followed by a catalytic domain, and a short vestige of the hinge region. MMP26 is apparently not glycosylated, and is a secreted MMP. Tissue analysis shows MMP26 most strongly in placenta and uterus, but also in kidney cells, lung cells, lymphocytes and lung or endometrial carcinoma cells. MMP26 is proteolytically active, cleaving casein in zymograms, and gelatin, a1PI, fibrinogen, fibronectin, vitronectin, type IV collagen, and apparently activating MMP9.
UOM: 1 * 100 µl


Código de Artigo: (ENZOALX804421R100)
Fornecedor: ENZO LIFE SCIENCES
Descrição: The aryl hydrocarbon receptor (AhR), also known as the dioxin receptor, is a ligand-activated helix/loop/helix transcription factor found in a variety of vertebrate species. The known ligands for AhR are foreign planar aromatic compounds, such as polycyclic aromatic compounds and halogenated aromatic compounds such as 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Unlike the steroid/thyroid hormone receptors, there is no known physiological ligand for the Ah Receptor.
Studies indicate that in non-ligand activated cells, AhR is found complexed with HSP90 predominantly in the cytoplasm. Upon binding to an agonist, the ligand-activated AhR is believed to transform to a nuclear, DNA binding form. This transformation process appears to involve dissociation of HSP90 from AhR followed by formation of a heterodimer with AhR nuclear translocator protein (Arnt). The AhR-ligand complex appears to initiate gene transcription of cytochrome P450 1A1.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-11719R-CY7)
Fornecedor: Bioss
Descrição: Calcyon is a single transmembrane protein that interacts with D1 dopamine receptors. Dopamine is a neurotransmitter that regulates synaptic transmission involved in learning and memory. D1 receptors, the most abundant dopamine receptor in the central nervous system, appear to modulate the activity of D2 dopamine receptors, mediate various behavioural responses, and regulate neuron growth and differentiation. Calcyon is present in neuronal cell bodies and processes of the cortex and hippocampus, and it is especially abundant in pyramidal neurons. Interaction of Calcyon with D1 receptors results in a release of intracellular calcium.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-11719R-CY3)
Fornecedor: Bioss
Descrição: Calcyon is a single transmembrane protein that interacts with D1 dopamine receptors. Dopamine is a neurotransmitter that regulates synaptic transmission involved in learning and memory. D1 receptors, the most abundant dopamine receptor in the central nervous system, appear to modulate the activity of D2 dopamine receptors, mediate various behavioural responses, and regulate neuron growth and differentiation. Calcyon is present in neuronal cell bodies and processes of the cortex and hippocampus, and it is especially abundant in pyramidal neurons. Interaction of Calcyon with D1 receptors results in a release of intracellular calcium.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-1473R-A555)
Fornecedor: Bioss
Descrição: This protein belongs to the subfamily of small cytokine CC proteins. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterised by two adjacent cysteines. This cytokine displays chemotactic activity for resting CD4 or CD8 T cells and eosinophils and binds to chemokine receptors CCR3 and CCR10. It induces calcium mobilisation in a dose-dependent manner. This chemokine may play a role in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-5179R-A680)
Fornecedor: Bioss
Descrição: Vital cellular functions such as cell proliferation and signal transduction are regulated in part by the balance between the activities of protein tyrosine kinases (PTK) and protein tyrosine phosphatases (PTPs). The protein contains a 121 residue extracellular domain, a single transmembrane segment, and 2 tandem intracytoplasmic catalytic domains. The PTP alpha protein is ubiquitously expressed and may play a fundamental role in the physiology of all cells.
UOM: 1 * 100 µl


Código de Artigo: (BOSSBS-5175R-A750)
Fornecedor: Bioss
Descrição: Vital cellular functions such as cell proliferation and signal transduction are regulated in part by the balance between the activities of protein tyrosine kinases (PTK) and protein tyrosine phosphatases (PTPs). The protein contains a 121 residue extracellular domain, a single transmembrane segment, and 2 tandem intracytoplasmic catalytic domains. The PTP alpha protein is ubiquitously expressed and may play a fundamental role in the physiology of all cells.
UOM: 1 * 100 µl


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O stock para este item é limitado. Por favor, certifique-se de que efetuou o seu login para visualizar o stock disponível. Se a call está visível e precisar de ajuda, por favor, ligue para 213 600 770
Este produto é sujeito a regulamentação especifica.
Em caso de encomenda, será contactado a solicitar documentação complementar necessária e/ou obrigatória (licença, autorização ou declaração de uso final) para a continuidade do pedido. Agradecemos a vossa compreensão
Este produto é sujeito a regulamentação especifica.
Em caso de encomenda, será contactado a solicitar documentação complementar necessária e/ou obrigatória (licença, autorização ou declaração de uso final) para a continuidade do pedido. Agradecemos a vossa compreensão.
Este produto está bloqueado. Para obter mais informações, contacte a VWR através do número 213 600 770.
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Este produto encontra-se em rutura de stock. Poderá encontrar alternativas pesquisando pelo código de artigo indicado acima. Se precisar de ajuda, por favor contacte a VWR através do 213 600 770.
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