Recombinant Proteins

Recombinant Proteins

Descrizione	Azione
Delta-like protein 1 (DLL1) is a type I transmembrane protein that belongs to the Delta/Serrate/Lag2 (DSL) family of Notch ligands. Mature human DLL1 consists of a 528 amino acid (aa) extracellular domain (ECD) with one DSL domain and eight EGF-like repeats, a 23 aa transmembrane segment, and a 155 aa cytoplasmic domain. Within the ECD, human DLL1 shares 91% aa sequence identity with mouse and rat DLL1. The residual membranebound portion of DLL1 can be cleave by presenilin-dependent γ-secretase, enabling the cytoplasmic domain to migrate to the nucleus. DLL1 localizes to adherens junctions on neuronal processes through its association with the scaffolding protein MAGI1. DLL1 is widely expressed, and it plays an important role in embryonic somite formation, cochlear hair cell differentiation, plus B and T lymphocyte differentiation. The upregulation of DLL1 in arterial endothelial cells following injury or angiogenic stimulation is central to postnatal arteriogenesis. DLL1 is also overexpressed in cervical carcinoma and glioma and contributes to tumor progression. Recombinant Human DLL1/Delta-1 Protein (His Tag) Codice: PKSH033699_10μg Confezionamento: 10μg	Dettagli
Delta-like protein 1 (DLL1) is a type I transmembrane protein that belongs to the Delta/Serrate/Lag2 (DSL) family of Notch ligands. Mature human DLL1 consists of a 528 amino acid (aa) extracellular domain (ECD) with one DSL domain and eight EGF-like repeats, a 23 aa transmembrane segment, and a 155 aa cytoplasmic domain. Within the ECD, human DLL1 shares 91% aa sequence identity with mouse and rat DLL1. The residual membranebound portion of DLL1 can be cleave by presenilin-dependent γ-secretase, enabling the cytoplasmic domain to migrate to the nucleus. DLL1 localizes to adherens junctions on neuronal processes through its association with the scaffolding protein MAGI1. DLL1 is widely expressed, and it plays an important role in embryonic somite formation, cochlear hair cell differentiation, plus B and T lymphocyte differentiation. The upregulation of DLL1 in arterial endothelial cells following injury or angiogenic stimulation is central to postnatal arteriogenesis. DLL1 is also overexpressed in cervical carcinoma and glioma and contributes to tumor progression. Recombinant Human DLL1/Delta-1 Protein (His Tag) Codice: PKSH033699_50μg Confezionamento: 50μg	Dettagli
Delta-like protein 1(DLL1) , also known as Delta1 , a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains , acts as a ligand for Notch receptors , and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor , and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway , whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells , DLL1 is constitutively cleaved by ADAM12 , and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent , takes place in cis orientation , and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1 , but not its N-or C-terminal proteolytic fragment , co-immunoprecipitates with ADAM12. By using a Notch reporter construct , we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore , ADAM9 and ADAM17 have the ability to process DLL1. In contrast , ADAM15 does not cleave DLL1 , although the two proteins still co-immunoprecipitate with each other. During fetal development , DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries. Recombinant Human DLL1 Protein(Fc Tag) Codice: PDMH100302_100μg Confezionamento: 100μg	Dettagli
Delta-like protein 1(DLL1) , also known as Delta1 , a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains , acts as a ligand for Notch receptors , and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor , and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway , whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells , DLL1 is constitutively cleaved by ADAM12 , and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent , takes place in cis orientation , and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1 , but not its N-or C-terminal proteolytic fragment , co-immunoprecipitates with ADAM12. By using a Notch reporter construct , we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore , ADAM9 and ADAM17 have the ability to process DLL1. In contrast , ADAM15 does not cleave DLL1 , although the two proteins still co-immunoprecipitate with each other. During fetal development , DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries. Recombinant Human DLL1 Protein(Fc Tag) Codice: PDMH100302_500μg Confezionamento: 500μg	Dettagli
Delta-like protein 1(DLL1) , also known as Delta1 , a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains , acts as a ligand for Notch receptors , and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor , and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway , whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells , DLL1 is constitutively cleaved by ADAM12 , and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent , takes place in cis orientation , and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1 , but not its N-or C-terminal proteolytic fragment , co-immunoprecipitates with ADAM12. By using a Notch reporter construct , we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore , ADAM9 and ADAM17 have the ability to process DLL1. In contrast , ADAM15 does not cleave DLL1 , although the two proteins still co-immunoprecipitate with each other. During fetal development , DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries. Recombinant Human DLL1 Protein(Fc Tag) Codice: PDMH100302_20μg Confezionamento: 20μg	Dettagli
Delta-like protein 1(DLL1) , also known as Delta1 , a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains , acts as a ligand for Notch receptors , and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor , and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway , whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells , DLL1 is constitutively cleaved by ADAM12 , and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent , takes place in cis orientation , and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1 , but not its N-or C-terminal proteolytic fragment , co-immunoprecipitates with ADAM12. By using a Notch reporter construct , we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore , ADAM9 and ADAM17 have the ability to process DLL1. In contrast , ADAM15 does not cleave DLL1 , although the two proteins still co-immunoprecipitate with each other. During fetal development , DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries. Recombinant Human DLL1 Protein(Fc Tag) Codice: PDMH100302_1mg Confezionamento: 1mg	Dettagli
Delta-like protein 1(DLL1) , also known as Delta1 , a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains , acts as a ligand for Notch receptors , and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor , and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway , whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells , DLL1 is constitutively cleaved by ADAM12 , and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent , takes place in cis orientation , and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1 , but not its N-or C-terminal proteolytic fragment , co-immunoprecipitates with ADAM12. By using a Notch reporter construct , we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore , ADAM9 and ADAM17 have the ability to process DLL1. In contrast , ADAM15 does not cleave DLL1 , although the two proteins still co-immunoprecipitate with each other. During fetal development , DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries. Recombinant Human DLL1 Protein(His Tag) Codice: PDMH100303_100μg Confezionamento: 100μg	Dettagli
Delta-like protein 1(DLL1) , also known as Delta1 , a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains , acts as a ligand for Notch receptors , and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor , and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway , whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells , DLL1 is constitutively cleaved by ADAM12 , and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent , takes place in cis orientation , and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1 , but not its N-or C-terminal proteolytic fragment , co-immunoprecipitates with ADAM12. By using a Notch reporter construct , we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore , ADAM9 and ADAM17 have the ability to process DLL1. In contrast , ADAM15 does not cleave DLL1 , although the two proteins still co-immunoprecipitate with each other. During fetal development , DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries. Recombinant Human DLL1 Protein(His Tag) Codice: PDMH100303_1mg Confezionamento: 1mg	Dettagli
Delta-like protein 1(DLL1) , also known as Delta1 , a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains , acts as a ligand for Notch receptors , and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor , and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway , whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells , DLL1 is constitutively cleaved by ADAM12 , and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent , takes place in cis orientation , and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1 , but not its N-or C-terminal proteolytic fragment , co-immunoprecipitates with ADAM12. By using a Notch reporter construct , we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore , ADAM9 and ADAM17 have the ability to process DLL1. In contrast , ADAM15 does not cleave DLL1 , although the two proteins still co-immunoprecipitate with each other. During fetal development , DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries. Recombinant Human DLL1 Protein(His Tag) Codice: PDMH100303_20μg Confezionamento: 20μg	Dettagli
Delta-like protein 1(DLL1) , also known as Delta1 , a single-pass type I membrane protein which contains one DSL domain and eight EGF-like domains , acts as a ligand for Notch receptors , and positively regulates T-cell development. DLL1 is proteolytically processed in a similar manner to the Notch receptor , and it has been speculated to participate in bidirectional signaling. The proteolytic processing of DLL1 helps achieve an asymmetry in Notch signaling in initially equivalent myogenic cells and helps sustain the balance between differentiation and self-renewal. Interactions between DLL1 and Notch in trans activate the Notch pathway , whereas DLL1 binding to Notch in cis inhibits Notch signaling. DLL1 undergoes proteolytic processing in its extracellular domain by ADAM10. It had been demonstrated that DLL1 represents a substrate for several other members of the ADAM family. In co-transfected cells , DLL1 is constitutively cleaved by ADAM12 , and the N-terminal fragment of DLL1 is released to medium. ADAM12-mediated cleavage of DLL1 is cell density-dependent , takes place in cis orientation , and does not require the presence of the cytoplasmic domain of ADAM12. Full-length DLL1 , but not its N-or C-terminal proteolytic fragment , co-immunoprecipitates with ADAM12. By using a Notch reporter construct , we show that DLL1 processing by ADAM12 increases Notch signaling in a cell-autonomous manner. Furthermore , ADAM9 and ADAM17 have the ability to process DLL1. In contrast , ADAM15 does not cleave DLL1 , although the two proteins still co-immunoprecipitate with each other. During fetal development , DLL1 is an essential Notch ligand in the vascular endothelium of large arteries to activate Notch1 and maintain arterial identity. DLL1-Notch signaling was required for VEGF receptor expression in fetal arteries. Recombinant Human DLL1 Protein(His Tag) Codice: PDMH100303_500μg Confezionamento: 500μg	Dettagli
Delta-like protein 4 (DLL4; Delta4); a type I membrane-bound Notch ligand; is one of five known Notch ligands in mammals and interacts predominantly with Notch 1; which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth; forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore; the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions; such as cancer; DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis; but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies; blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density; yet causes marked growth inhibition due to functionally defective vasculature. Thus; DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy. Recombinant Human DLL4 Protein (Fc Tag) Codice: PKSH031806_50μg Confezionamento: 50μg	Dettagli
Delta-like protein 4 (DLL4; Delta4); a type I membrane-bound Notch ligand; is one of five known Notch ligands in mammals and interacts predominantly with Notch 1; which has a key role in vascular development. Recent studies yield substantial insights into the role of DLL4 in angiogenesis. DLL4 is induced by vascular endothelial growth factor (VEGF) and acts downstream of VEGF as a 'brake' on VEGF-induced vessel growth; forming an autoregulatory negative feedback loop inactivating VEGF. DLL4 is downstream of VEGF signaling and its activation triggers a negative feedback that restrains the effects of VEGF. Attenuation of DLL4/Notch signaling results in chaotic vascular network with excessive branching and sprouting. DLL4 is widely distributed in tissues other than vessels including many malignancies. Furthermore; the molecule is internalized on binding its receptor and often transported to the nucleus. In pathological conditions; such as cancer; DLL4 is up-regulated strongly in the tumour vasculature. Blockade of DLL4-mediated Notch signaling strikingly increases nonproductive angiogenesis; but significantly inhibits tumor growth in preclinical mouse models. In preclinical studies; blocking of DLL4/Notch signaling is associated with a paradoxical increase in tumor vessel density; yet causes marked growth inhibition due to functionally defective vasculature. Thus; DLL4 blockade holds promise as an additional strategy for angiogenesis-based cancer therapy. Recombinant Human DLL4 Protein (Fc Tag) Codice: PKSH031806_500μg Confezionamento: 500μg	Dettagli

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