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Catalog Number: (BOSSBS-6792R)
Supplier: Bioss
Description: The mammalian homologues of the key cell death gene CED 4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease activating factor 1). Apaf1 binds to cytochrome c (Apaf2) and caspase 9 (Apaf3), which leads to caspase 9 activation. Activated caspase 9 in turn cleaves and activates caspase 3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. A new Apaf1 Interacting Protein (APIP) also known as CG129 and MMRP19, has been identified as a negative regulator of ischemic injury. APIP competes with Caspase 9 binding site of Apaf1. APIP is predicted to code for a 204 amino acid. An isoform of APIP, APIP2 encodes a 242 amino acid protein, which is an alternative splicing variant differing in its N terminus from APIP. APIP transcript is ubiquitously expressed in most adult tissue with high expression in skeletal muscle, heart, and kidney.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6792R-CY3)
Supplier: Bioss
Description: The mammalian homologues of the key cell death gene CED 4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease activating factor 1). Apaf1 binds to cytochrome c (Apaf2) and caspase 9 (Apaf3), which leads to caspase 9 activation. Activated caspase 9 in turn cleaves and activates caspase 3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. A new Apaf1 Interacting Protein (APIP) also known as CG129 and MMRP19, has been identified as a negative regulator of ischemic injury. APIP competes with Caspase 9 binding site of Apaf1. APIP is predicted to code for a 204 amino acid. An isoform of APIP, APIP2 encodes a 242 amino acid protein, which is an alternative splicing variant differing in its N terminus from APIP. APIP transcript is ubiquitously expressed in most adult tissue with high expression in skeletal muscle, heart, and kidney.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6792R-A750)
Supplier: Bioss
Description: The mammalian homologues of the key cell death gene CED 4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease activating factor 1). Apaf1 binds to cytochrome c (Apaf2) and caspase 9 (Apaf3), which leads to caspase 9 activation. Activated caspase 9 in turn cleaves and activates caspase 3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. A new Apaf1 Interacting Protein (APIP) also known as CG129 and MMRP19, has been identified as a negative regulator of ischemic injury. APIP competes with Caspase 9 binding site of Apaf1. APIP is predicted to code for a 204 amino acid. An isoform of APIP, APIP2 encodes a 242 amino acid protein, which is an alternative splicing variant differing in its N terminus from APIP. APIP transcript is ubiquitously expressed in most adult tissue with high expression in skeletal muscle, heart, and kidney.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6792R-A488)
Supplier: Bioss
Description: The mammalian homologues of the key cell death gene CED 4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease activating factor 1). Apaf1 binds to cytochrome c (Apaf2) and caspase 9 (Apaf3), which leads to caspase 9 activation. Activated caspase 9 in turn cleaves and activates caspase 3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. A new Apaf1 Interacting Protein (APIP) also known as CG129 and MMRP19, has been identified as a negative regulator of ischemic injury. APIP competes with Caspase 9 binding site of Apaf1. APIP is predicted to code for a 204 amino acid. An isoform of APIP, APIP2 encodes a 242 amino acid protein, which is an alternative splicing variant differing in its N terminus from APIP. APIP transcript is ubiquitously expressed in most adult tissue with high expression in skeletal muscle, heart, and kidney.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-2002R-A750)
Supplier: Bioss
Description: Influenza A virus is a major public health threat. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalisation of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Influenza A Virus (strain swl A/California/04/2009 H1N1).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-5387R-A680)
Supplier: Bioss
Description: Reversible acetylation of highly conserved lysine residues within the N-terminal tail domains of core histones, plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone acetylation is a dynamic process determined by the net activities of histone acetyltransferases (HATs) and the competing enzymes histone deacetylases (HDACs). Histone deacetylases activities are often, but not always, associated with transcriptional repression and nucleosomal condensations. Recruitment of the multiprotein complexes to promoter sites occurs by many sequence specific DNA-binding proteins such as unliganded nuclear hormone receptors, DP1-E2F, YY1 and Rb family of transcription factors, transcriptional repressors and tumor suppressors (e.g. BRCA1). Aberrant recruitment of HDACs by certain oncoproteins may occur in certain neoplastic diseases. Belongs to the histone deacetylase family.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-5425R-HRP)
Supplier: Bioss
Description: MAX protein is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms provides a complex system of transcriptional regulation. Mutations of this gene have been reported to be associated with hereditary pheochromocytoma. A pseudogene of this gene is located on the long arm of chromosome 7. Alternative splicing results in multiple transcript variants.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11260R-A680)
Supplier: Bioss
Description: Members of the transforming growth factor-beta (TGF-Beta) superfamily play critical roles in controlling cell growth and differentiation. Effects of TGF-Beta family ligands are mediated by Smad proteins. The Smad nuclear interacting protein (SNIP1) contains a forkhead-associated (FHA) domain and acts as a nuclear inhibitor of CBP/p300. SNIP1 potently inhibits the activity of NF-kappa B, which binds the C/H1 domain of CBP/p300, by competing for the binding site. SNIP1 is also thought to induce expression of Cyclin D1 to promote cellular proliferation. SNIP1 is ubiquitously expressed with high expression in heart and skeletal muscle.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11260R-A750)
Supplier: Bioss
Description: Members of the transforming growth factor-beta (TGF-Beta) superfamily play critical roles in controlling cell growth and differentiation. Effects of TGF-Beta family ligands are mediated by Smad proteins. The Smad nuclear interacting protein (SNIP1) contains a forkhead-associated (FHA) domain and acts as a nuclear inhibitor of CBP/p300. SNIP1 potently inhibits the activity of NF-kappa B, which binds the C/H1 domain of CBP/p300, by competing for the binding site. SNIP1 is also thought to induce expression of Cyclin D1 to promote cellular proliferation. SNIP1 is ubiquitously expressed with high expression in heart and skeletal muscle.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11260R-CY3)
Supplier: Bioss
Description: Members of the transforming growth factor-beta (TGF-Beta) superfamily play critical roles in controlling cell growth and differentiation. Effects of TGF-Beta family ligands are mediated by Smad proteins. The Smad nuclear interacting protein (SNIP1) contains a forkhead-associated (FHA) domain and acts as a nuclear inhibitor of CBP/p300. SNIP1 potently inhibits the activity of NF-kappa B, which binds the C/H1 domain of CBP/p300, by competing for the binding site. SNIP1 is also thought to induce expression of Cyclin D1 to promote cellular proliferation. SNIP1 is ubiquitously expressed with high expression in heart and skeletal muscle.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6792R-CY5)
Supplier: Bioss
Description: The mammalian homologues of the key cell death gene CED 4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease activating factor 1). Apaf1 binds to cytochrome c (Apaf2) and caspase 9 (Apaf3), which leads to caspase 9 activation. Activated caspase 9 in turn cleaves and activates caspase 3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. A new Apaf1 Interacting Protein (APIP) also known as CG129 and MMRP19, has been identified as a negative regulator of ischemic injury. APIP competes with Caspase 9 binding site of Apaf1. APIP is predicted to code for a 204 amino acid. An isoform of APIP, APIP2 encodes a 242 amino acid protein, which is an alternative splicing variant differing in its N terminus from APIP. APIP transcript is ubiquitously expressed in most adult tissue with high expression in skeletal muscle, heart, and kidney.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-6792R-A680)
Supplier: Bioss
Description: The mammalian homologues of the key cell death gene CED 4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease activating factor 1). Apaf1 binds to cytochrome c (Apaf2) and caspase 9 (Apaf3), which leads to caspase 9 activation. Activated caspase 9 in turn cleaves and activates caspase 3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. A new Apaf1 Interacting Protein (APIP) also known as CG129 and MMRP19, has been identified as a negative regulator of ischemic injury. APIP competes with Caspase 9 binding site of Apaf1. APIP is predicted to code for a 204 amino acid. An isoform of APIP, APIP2 encodes a 242 amino acid protein, which is an alternative splicing variant differing in its N terminus from APIP. APIP transcript is ubiquitously expressed in most adult tissue with high expression in skeletal muscle, heart, and kidney.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11542R)
Supplier: Bioss
Description: Calcineurin is a Ca(2+) dependent protein phosphatase that is involed in several neuornal functions. Proteins belonging to the RCAN (Regulator of calcineurin) family modulate the activity of Calcineurin through a valine-rich region within their carboxyl tail. RCANs compete with NFATs (Nuclear factor of activated T-cells) for binding to the same docking site in calcineurin, which results in either inhibition or activation of calcineurin activity. Calcipressin-2, also known as RCAN2 and DSCR1L1 (Down syndrome candidate region 1-like 1), is a 197 amino acid protein that is highly expressed in both the cytoplasm and nucleus of neurons and is the only RCAN family member that is found in glial cells. Calcipressin-3, also known as RCAN3 and DSCR1L2 (Down syndrome candidate region 1-like protein 2), is a 241 amino acid protein that potentially is involved in central nervous system development. Calcipressin-3 interacts with cardiac troponin I, suggesting that it may play a role in cardiac contraction events.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1300R-A350)
Supplier: Bioss
Description: Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1300R-A680)
Supplier: Bioss
Description: Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1300R-FITC)
Supplier: Bioss
Description: Tyrosine-protein kinase that acts as cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of proinflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at eurega_services@eu.vwr.com
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