Recherche de texte >
acids+and+salts+high+purity
Imprimer
Votre recherche pour:
149 650 les résultats ont été trouvés
acids+and+salts+high+purity
Numéro de catalogue:
(BOSSBS-9704R-A680)
Fournisseur:
Bioss
Description:
The Interferon family of proteins are able to alter the expression of a variety of target genes, thereby controlling various events within the cell. IFI-35 (Interferon-induced 35 kDa protein), also known as IFP35, is a 286 amino acid interferon-induced protein. localised to the nucleus and expressed in macrophages, fibroblasts and epithelial cells, IFI-35 is a leucine zipper protein that can form homodimers, but, unlike most leucine zipper proteins, cannot bind DNA. Upon induction by IFN-? IFI-35 associates with Nmi (N-Myc-interacting protein), resulting in the formation of a high molecular weight complex that is thought to play a role in IFN Signalling and cellular responses. Once complexed with Nmi, IFI-35 is unable to be degraded by the proteasome, suggesting that IFI-35 is protected from degradation only when needed by IFN Two isoforms of IFI-35 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9704R-A750)
Fournisseur:
Bioss
Description:
The Interferon family of proteins are able to alter the expression of a variety of target genes, thereby controlling various events within the cell. IFI-35 (Interferon-induced 35 kDa protein), also known as IFP35, is a 286 amino acid interferon-induced protein. localised to the nucleus and expressed in macrophages, fibroblasts and epithelial cells, IFI-35 is a leucine zipper protein that can form homodimers, but, unlike most leucine zipper proteins, cannot bind DNA. Upon induction by IFN-? IFI-35 associates with Nmi (N-Myc-interacting protein), resulting in the formation of a high molecular weight complex that is thought to play a role in IFN Signalling and cellular responses. Once complexed with Nmi, IFI-35 is unable to be degraded by the proteasome, suggesting that IFI-35 is protected from degradation only when needed by IFN Two isoforms of IFI-35 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9704R-CY7)
Fournisseur:
Bioss
Description:
The Interferon family of proteins are able to alter the expression of a variety of target genes, thereby controlling various events within the cell. IFI-35 (Interferon-induced 35 kDa protein), also known as IFP35, is a 286 amino acid interferon-induced protein. Localized to the nucleus and expressed in macrophages, fibroblasts and epithelial cells, IFI-35 is a leucine zipper protein that can form homodimers, but, unlike most leucine zipper proteins, cannot bind DNA. Upon induction by IFN-? IFI-35 associates with Nmi (N-Myc-interacting protein), resulting in the formation of a high molecular weight complex that is thought to play a role in IFN-?signaling and cellular responses. Once complexed with Nmi, IFI-35 is unable to be degraded by the proteasome, suggesting that IFI-35 is protected from degradation only when needed by IFN-? Two isoforms of IFI-35 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-9704R)
Fournisseur:
Bioss
Description:
The Interferon family of proteins are able to alter the expression of a variety of target genes, thereby controlling various events within the cell. IFI-35 (Interferon-induced 35 kDa protein), also known as IFP35, is a 286 amino acid interferon-induced protein. Localized to the nucleus and expressed in macrophages, fibroblasts and epithelial cells, IFI-35 is a leucine zipper protein that can form homodimers, but, unlike most leucine zipper proteins, cannot bind DNA. Upon induction by IFN-? IFI-35 associates with Nmi (N-Myc-interacting protein), resulting in the formation of a high molecular weight complex that is thought to play a role in IFN-?signaling and cellular responses. Once complexed with Nmi, IFI-35 is unable to be degraded by the proteasome, suggesting that IFI-35 is protected from degradation only when needed by IFN-? Two isoforms of IFI-35 exist due to alternative splicing events.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6792R-HRP)
Fournisseur:
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
Numéro de catalogue:
(BOSSBS-6792R-A647)
Fournisseur:
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
Numéro de catalogue:
(BOSSBS-6792R-A555)
Fournisseur:
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
Numéro de catalogue:
(BOSSBS-5808R-HRP)
Fournisseur:
Bioss
Description:
CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5808R-FITC)
Fournisseur:
Bioss
Description:
CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11959R-CY3)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK5 (SLIT and NTRK-like family, member 5), also known as LRRC11 (leucine-rich repeat-containing protein 11), is a 958 amino acid single-pass type I membrane protein that contains 16 LRR repeats and belongs to the SLITRK family. Expressed at high levels in the cerebral cortex, but also present in areas of the spinal cord and medulla, SLITRK5 functions to suppress neurite outgrowth, thereby playing a regulatory role in neuronal function. The gene encoding SLITRK5 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome. Trisomy 13, also known as Patau syndrome, is deadly and the few who survive past one year suffer from permanent neurologic defects, difficulty eating and vulnerability to serious respiratory infections.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11959R-A750)
Fournisseur:
Bioss
Description:
The leucine-rich (LRR) repeat is a 20 to 30 amino acid motif that forms a hydrophobic å/ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. SLITRK5 (SLIT and NTRK-like family, member 5), also known as LRRC11 (leucine-rich repeat-containing protein 11), is a 958 amino acid single-pass type I membrane protein that contains 16 LRR repeats and belongs to the SLITRK family. Expressed at high levels in the cerebral cortex, but also present in areas of the spinal cord and medulla, SLITRK5 functions to suppress neurite outgrowth, thereby playing a regulatory role in neuronal function. The gene encoding SLITRK5 maps to human chromosome 13, which houses over 400 genes, such as BRCA2 and RB1, and comprises nearly 4% of the human genome. Trisomy 13, also known as Patau syndrome, is deadly and the few who survive past one year suffer from permanent neurologic defects, difficulty eating and vulnerability to serious respiratory infections.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This antibody recognizes a protein of 54 kDa, which is identified as AMACR, also known as p504S. It is an enzyme that is involved in bile acid biosynthesis and β-oxidation of branched-chain fatty acids. AMACR is essential in lipid metabolism. It is expressed in cells of premalignant high-grade prostatic intraepithelial neoplasia (HGPIN) and prostate adenocarcinoma. The majority of the carcinoma cells show a distinct granular cytoplasmic staining reaction. AMACR is present at low or undetectable levels in glandular epithelial cells of normal prostate and benign prostatic hyperplasia. A spotty granular cytoplasmic staining is seen in a few cells of the benign glands. AMACR is expressed in normal liver (hepatocytes), kidney (tubular epithelial cells) and gall bladder (epithelial cells). Expression has also been found in lung (bronchial epithelial cells) and colon (colonic surface epithelium). AMACR expression can also be found in hepatocellular carcinoma and kidney carcinoma. Past studies have also shown that AMACR is expressed in various colon carcinomas (well, moderately and poorly differentiated) and overexpressed in prostate carcinoma.
Fournisseur:
Biotium
Description:
This antibody recognizes a protein of 54 kDa, which is identified as AMACR, also known as p504S. It is an enzyme that is involved in bile acid biosynthesis and β-oxidation of branched-chain fatty acids. AMACR is essential in lipid metabolism. It is expressed in cells of premalignant high-grade prostatic intraepithelial neoplasia (HGPIN) and prostate adenocarcinoma. The majority of the carcinoma cells show a distinct granular cytoplasmic staining reaction. AMACR is present at low or undetectable levels in glandular epithelial cells of normal prostate and benign prostatic hyperplasia. A spotty granular cytoplasmic staining is seen in a few cells of the benign glands. AMACR is expressed in normal liver (hepatocytes), kidney (tubular epithelial cells) and gall bladder (epithelial cells). Expression has also been found in lung (bronchial epithelial cells) and colon (colonic surface epithelium). AMACR expression can also be found in hepatocellular carcinoma and kidney carcinoma. Past studies have also shown that AMACR is expressed in various colon carcinomas (well, moderately and poorly differentiated) and overexpressed in prostate carcinoma.
Fournisseur:
Biotium
Description:
This antibody recognizes a protein of 54 kDa, which is identified as AMACR, also known as p504S. It is an enzyme that is involved in bile acid biosynthesis and β-oxidation of branched-chain fatty acids. AMACR is essential in lipid metabolism. It is expressed in cells of premalignant high-grade prostatic intraepithelial neoplasia (HGPIN) and prostate adenocarcinoma. The majority of the carcinoma cells show a distinct granular cytoplasmic staining reaction. AMACR is present at low or undetectable levels in glandular epithelial cells of normal prostate and benign prostatic hyperplasia. A spotty granular cytoplasmic staining is seen in a few cells of the benign glands. AMACR is expressed in normal liver (hepatocytes), kidney (tubular epithelial cells) and gall bladder (epithelial cells). Expression has also been found in lung (bronchial epithelial cells) and colon (colonic surface epithelium). AMACR expression can also be found in hepatocellular carcinoma and kidney carcinoma. Past studies have also shown that AMACR is expressed in various colon carcinomas (well, moderately and poorly differentiated) and overexpressed in prostate carcinoma.
Fournisseur:
Quantabio
Description:
Rapid extraction and purification of high-quality total RNA from cultured cells or tissue.
Fournisseur:
Bernd Kraft
Description:
Sodium thiosulfate 0.22 mol/l (0.22 N) en solution aqueuse
Appel de prix
Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'
 est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'
est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
Ces articles ne peuvent être ajoutés au Panier. Veuillez contacter votre service client ou envoyer un e-mail à vwr.be@vwr.com
Une documentation supplémentaire peut être nécessaire pour l'achat de cet article. Un représentant de VWR vous contactera si nécessaire.
Ce produit a été bloqué par votre organisation. Contacter votre service d'achat pour plus d'informations.
Le produit original n'est plus disponible. Le remplacement représenté est disponible
Les produits marqués de ce symbole ne seront bientôt plus disponibles - vente jusqu'à épuisement de stock. Des alternatives peuvent être disponibles en recherchant le code article VWR indiqué ci-dessus. Si vous avez besoin d'une assistance supplémentaire, veuillez contacter notre Service Clientèle au 016 385 011.
|
|||||||||
Vue liste
