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acids+and+salts+high+purity
Numéro de catalogue:
(BTIUBNUM0879-50)
Fournisseur:
Biotium
Description:
Recognizes a protein of 57 kDa, identified as p57Kip2. It shows no cross-reaction with p27Kip1. p57Kip2 is a potent tight-binding inhibitor of several G1 cyclin complexes, and is a negative regulator of cell proliferation. Anti-p57 has been used as an aide in identification of complete hydatidiform mole (CHM) (no nuclear labeling of cytotrophoblasts and stromal cells) from partial hydatidiform mole (PHM) in which both cytotrophoblasts and stromal cells stain. The histological differentiation of complete mole, partial mole, and hydropic spontaneous abortion is problematic. Most complete hydatidiform moles are diploid, whereas most partial moles are triploid. Ploidy studies will identify partial moles, but will not differentiate complete moles from non-molar gestations. Complete moles carry a high risk of persistent disease and choriocarcinoma, while partial moles have a very low risk. In normal placenta, many cytotrophoblast nuclei and stromal cells are labeled with this antibody. Similar findings apply to PHM and hydropic abortus tissues. Intervillous trophoblastic islands (IVTIs) demonstrate nuclear labeling in all three entities and serve as an internal control.
UOM:
1 * 50 µl
Fournisseur:
Biotium
Description:
Recognizes a protein of 57 kDa, identified as p57Kip2. It shows no cross-reaction with p27Kip1. p57Kip2 is a potent tight-binding inhibitor of several G1 cyclin complexes, and is a negative regulator of cell proliferation. Anti-p57 has been used as an aide in identification of complete hydatidiform mole (CHM) (no nuclear labeling of cytotrophoblasts and stromal cells) from partial hydatidiform mole (PHM) in which both cytotrophoblasts and stromal cells stain. The histological differentiation of complete mole, partial mole, and hydropic spontaneous abortion is problematic. Most complete hydatidiform moles are diploid, whereas most partial moles are triploid. Ploidy studies will identify partial moles, but will not differentiate complete moles from non-molar gestations. Complete moles carry a high risk of persistent disease and choriocarcinoma, while partial moles have a very low risk. In normal placenta, many cytotrophoblast nuclei and stromal cells are labeled with this antibody. Similar findings apply to PHM and hydropic abortus tissues. Intervillous trophoblastic islands (IVTIs) demonstrate nuclear labeling in all three entities and serve as an internal control.
Numéro de catalogue:
(TCIAS0308-5ML)
Fournisseur:
TCI
Description:
Organic Standard, Methyl Decanoate, Purity (GC): min. 99.5 %, Type de conditionnement: Flacon Verre
UOM:
1 * 5 mL
Numéro de catalogue:
(BOSSBS-9072R-FITC)
Fournisseur:
Bioss
Description:
Hepatoma Derived Growth Factor (HDGF) is the original member of a family of polypeptides designated HDGF-related proteins (HRPs). HDGF was initially characterized as a secreted mitogen from the Huh-7 human hepatoma cell line. This nuclear targeted vascular smooth muscle cell mitogen (VSM) is a heparin-binding protein that is highly expressed in tumor cells where it stimulates proliferation. HDGF is also reported to be involved in organ development and lung remodeling after injury by promoting proliferation of lung epithelial cells. During development, HDGF expression is high in the nucleus and cytoplasm of smooth muscle and endothelial cells. The HRP (HDGF related proteins) family contains four proteins, HRP-1, HRP-2, HRP-3 and HRP-4. HRP-1 and HRP-4 are only expressed in testis while HRP-2 is widely expressed in different tissues. HRP-3 can solely be found in the nervous system. Specifically it is strongly expressed in bulbus, olfactorius, piriform cotrex and amygdala complex while HRP-2 in brain is located in the the thalamus, prefrontal and parietal cortex, neurohypophysis, and the cerebellum. In the central nervous system, HRP proteins are play a role in neuron proliferation and cell survival.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9072R-A647)
Fournisseur:
Bioss
Description:
Hepatoma Derived Growth Factor (HDGF) is the original member of a family of polypeptides designated HDGF-related proteins (HRPs). HDGF was initially characterized as a secreted mitogen from the Huh-7 human hepatoma cell line. This nuclear targeted vascular smooth muscle cell mitogen (VSM) is a heparin-binding protein that is highly expressed in tumor cells where it stimulates proliferation. HDGF is also reported to be involved in organ development and lung remodeling after injury by promoting proliferation of lung epithelial cells. During development, HDGF expression is high in the nucleus and cytoplasm of smooth muscle and endothelial cells. The HRP (HDGF related proteins) family contains four proteins, HRP-1, HRP-2, HRP-3 and HRP-4. HRP-1 and HRP-4 are only expressed in testis while HRP-2 is widely expressed in different tissues. HRP-3 can solely be found in the nervous system. Specifically it is strongly expressed in bulbus, olfactorius, piriform cotrex and amygdala complex while HRP-2 in brain is located in the the thalamus, prefrontal and parietal cortex, neurohypophysis, and the cerebellum. In the central nervous system, HRP proteins are play a role in neuron proliferation and cell survival.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-15371R-A488)
Fournisseur:
Bioss
Description:
Atypical chemokine receptor that controls chemokine levels and localisation via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalising receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalisation and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-15371R-CY7)
Fournisseur:
Bioss
Description:
Atypical chemokine receptor that controls chemokine levels and localisation via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalising receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalisation and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-15371R-A680)
Fournisseur:
Bioss
Description:
Atypical chemokine receptor that controls chemokine levels and localisation via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalising receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalisation and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8682R-A350)
Fournisseur:
Bioss
Description:
The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8682R-A488)
Fournisseur:
Bioss
Description:
The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4897R-CY3)
Fournisseur:
Bioss
Description:
Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4897R-CY5.5)
Fournisseur:
Bioss
Description:
Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1293R-A555)
Fournisseur:
Bioss
Description:
Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1293R-CY7)
Fournisseur:
Bioss
Description:
Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-4897R-FITC)
Fournisseur:
Bioss
Description:
Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.
UOM:
1 * 100 µl
Fournisseur:
ANSELL HEALTH CARE
Description:
Ces gants tricotés combinent une excellente résistance aux flammes, une protection élevée contre les coupures et une conception ergonomique. Le fil composite exclusif fabriqué en modacrylique, fibre de verre et Kevlar® offre une résistance exceptionnelle aux coupures pour une manipulation en toute sécurité d'objets et de matériaux pointus.
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