You Searched For: Phosphonitrilic+chloride+trimer

Catalog Number: (BOSSBS-12945R-A555)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11749R-A555)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4) is a putative member of a novel PP family. The PP2A family comprises subfamily members PP2Aå and PP2A∫. The PP2A catalytic subunit associates with a variety of regulatory subunits. The B family of regulatory subunits (including B55, B56 and PR72/130 subfamilies) is believed to participate in substrate specificity and catalytic activity. PP2A-B55, also known as PP2A regulatory subunit subfamily B55 or PP2A-B1, is a B subfamily consisting of four B55 isoforms (Alpha,Beta, Gamma and Delta) encoded by four distinct genes.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12945R-A647)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12944R-HRP)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11749R-A750)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4) is a putative member of a novel PP family. The PP2A family comprises subfamily members PP2Aå and PP2A. The PP2A catalytic subunit associates with a variety of regulatory subunits. The B family of regulatory subunits (including B55, B56 and PR72/130 subfamilies) is believed to participate in substrate specificity and catalytic activity. PP2A-B55, also known as PP2A regulatory subunit subfamily B55 or PP2A-B1, is a B subfamily consisting of four B55 isoforms (Alpha, Beta, Gamma and Delta) encoded by four distinct genes.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12945R-A680)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca²⁺-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca²⁺ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12945R-A488)

Supplier: Bioss

Description: Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11749R-HRP)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4) is a putative member of a novel PP family. The PP2A family comprises subfamily members PP2Aå and PP2A∫. The PP2A catalytic subunit associates with a variety of regulatory subunits. The B family of regulatory subunits (including B55, B56 and PR72/130 subfamilies) is believed to participate in substrate specificity and catalytic activity. PP2A-B55, also known as PP2A regulatory subunit subfamily B55 or PP2A-B1, is a B subfamily consisting of four B55 isoforms (Alpha,Beta, Gamma and Delta) encoded by four distinct genes.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11749R-FITC)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4) is a putative member of a novel PP family. The PP2A family comprises subfamily members PP2Aå and PP2A∫. The PP2A catalytic subunit associates with a variety of regulatory subunits. The B family of regulatory subunits (including B55, B56 and PR72/130 subfamilies) is believed to participate in substrate specificity and catalytic activity. PP2A-B55, also known as PP2A regulatory subunit subfamily B55 or PP2A-B1, is a B subfamily consisting of four B55 isoforms (Alpha,Beta, Gamma and Delta) encoded by four distinct genes.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11749R-A647)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4) is a putative member of a novel PP family. The PP2A family comprises subfamily members PP2Aå and PP2A∫. The PP2A catalytic subunit associates with a variety of regulatory subunits. The B family of regulatory subunits (including B55, B56 and PR72/130 subfamilies) is believed to participate in substrate specificity and catalytic activity. PP2A-B55, also known as PP2A regulatory subunit subfamily B55 or PP2A-B1, is a B subfamily consisting of four B55 isoforms (Alpha,Beta, Gamma and Delta) encoded by four distinct genes.

UOM: 1 * 100 µl

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Catalog Number: (HORI5200100690)

Supplier: HORIBA

Description: Solvent S-316 for oil extraction

UOM: 1 * 1,5 kg

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Catalog Number: (PRSI26-952)

Supplier: ProSci Inc.

Description: Replication protein A (RPA) is an essential factor for DNA double-strand break repair and cell cycle checkpoint activation. RPA4 is the 32-kDa subunit of the RPA, which associates with the 70- and 13-kDa subunits to form a trimeric RPA complex.Replication protein A (RPA) is an essential factor for DNA double-strand break repair and cell cycle checkpoint activation. This gene encodes the 32-kDa subunit of the RPA, which associates with the 70- and 13-kDa subunits to form a trimeric RPA complex.

UOM: 1 * 50 µG

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Catalog Number: (PRSI90-231)

Supplier: ProSci Inc.

Description: Tumour necrosis factor (TNF, cachexin or cachectin and formerly known as tumour necrosis factor-alpha) is a cytokine involved in systemic inflammation and is a member of a group of cytokines that stimulate the acute phase reaction. MultimericTNF-alpha™ is a high activity construct in which two trimeric TNF-alpha ligands are artificially linked via the collagen domain of ACRP30. The receptor TNF-R1 is activated by both the membrane-bound and soluble trimeric forms of TNF-alpha, whereas the receptor TNF-R2 only responds to the membrane-bound form of TNF-alpha (TNF-alpha (human) (multimeric) (rec. ) (Prod. No. AG-40B-0019). Since the MultimericTNF-alpha™ mimics the membrane-bound form (forms oligomers higher than trimer), it is the only TNF-alpha protein that can activate the TNF-R2. For TNF-R1 activation, either "normal" TNF-alpha or MultimericTNF-alpha™ can be used.

UOM: 1 * 10 µG

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Catalog Number: (PRSI27-320)

Supplier: ProSci Inc.

Description: NFYA is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.

UOM: 1 * 100 µG

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Catalog Number: (BOSSBS-2002R-A680)

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

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Catalog Number: (PRSI27-329)

Supplier: ProSci Inc.

Description: NFYA is one subunit of a trimeric complex, forming a highly conserved transcription factor that binds to CCAAT motifs in the promoter regions in a variety of genes. Subunit A associates with a tight dimer composed of the B and C subunits, resulting in a trimer that binds to DNA with high specificity and affinity. The sequence specific interactions of the complex are made by the A subunit, suggesting a role as the regulatory subunit. In addition, there is evidence of post-transcriptional regulation in this gene product, either by protein degradation or control of translation. Further regulation is represented by alternative splicing in the glutamine-rich activation domain, with clear tissue-specific preferences for the two isoforms.

UOM: 1 * 50 µG

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