Recherche de texte >
block+heaters+
Imprimer
Votre recherche pour:
7 827 les résultats ont été trouvés
block+heaters+
Numéro de catalogue:
(VERNA0C1S1520)
Fournisseur:
Saint Gobain Life Sciences
Description:
For UV inks in particular, UV blocking properties is an industry standard. Tygon® Ink 1000 has shown over an accelerated testing period that it can maintain the ink integrity with our patented technology, making it an ideal candidate for the UV market.
UOM:
1 * 15 m
New Product
Fournisseur:
ENZO LIFE SCIENCES
Description:
PAF receptor antagonist. Inhibits PAF-induced human platelet and neutrophil aggregation in vitro (IC50=0.17 and 0.36µM respectively). In vivo it dose dependently blocks eosinophil activation and displays antiallergic and anti-inflammatory activity in various models. Induces differentiation and triggers apoptosis and in a variety of cell lines.
Numéro de catalogue:
(BOSSBS-0738R-CY5)
Fournisseur:
Bioss
Description:
Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and NR2C2/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9. Isoform 1 blocks staurosporine-induced apoptosis. Isoform 2 blocks etoposide-induced apoptosis. Isoform 2 protects against natural killer (NK) cell killing whereas isoform 1 augments killing.
UOM:
1 * 100 µl
Numéro de catalogue:
(ENZOADI801928)
Fournisseur:
ENZO LIFE SCIENCES
Description:
This BSA Solution (10%) is specially designed to create the Blocking Buffer and Assay Buffer in ImmunoSet products. Each bottle is sufficient for use with 5×96 wells microtiter plates if following the instructions in our ImmunoSet protocol. The BSA Solution may be used for any other assay development needs. Additional assay development reagents are available as companion products to our ImmunoSet products.
UOM:
1 * 50 mL
New Product
Numéro de catalogue:
(BOSSBS-2789R-A350)
Fournisseur:
Bioss
Description:
Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-1 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2789R-A647)
Fournisseur:
Bioss
Description:
Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-1 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2789R-FITC)
Fournisseur:
Bioss
Description:
Involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. Also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. Inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. Inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP1 and prevents the conformational rearrangement of TAP induced by peptide binding. Inhibited by human adenovirus E3-19K glycoprotein, which binds the TAP complex and acts as a tapasin inhibitor, preventing MHC class I/TAP association. Expression of TAP1 is down-regulated by human Epstein-Barr virus vIL-1 protein, thereby affecting the transport of peptides into the endoplasmic reticulum and subsequent peptide loading by MHC class I molecules.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5161R-A555)
Fournisseur:
Bioss
Description:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5161R-A488)
Fournisseur:
Bioss
Description:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5161R-HRP)
Fournisseur:
Bioss
Description:
F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12215R-A750)
Fournisseur:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Kr_ppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. ZNF266 is a 549 amino acid nuclear protein belonging to the Kr_ppel C2H2-type zinc finger protein family. ZNF266 has one KRAB domain and fourteen C2H2 zinc fingers. Due to the presence of these domains, ZNF266 is thought to be involved in transcriptional regulation. Repression of ZNF266 results in the blocking of erythroid differentiation and partial blocking of megakaryocytic differentiation, possibly indicating a role in the differentiation of erythroids and megakaryocytes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12215R-A647)
Fournisseur:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. ZNF266 is a 549 amino acid nuclear protein belonging to the Krüppel C2H2-type zinc finger protein family. ZNF266 has one KRAB domain and fourteen C2H2 zinc fingers. Due to the presence of these domains, ZNF266 is thought to be involved in transcriptional regulation. Repression of ZNF266 results in the blocking of erythroid differentiation and partial blocking of megakaryocytic differentiation, possibly indicating a role in the differentiation of erythroids and megakaryocytes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-12215R-CY7)
Fournisseur:
Bioss
Description:
Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. ZNF266 is a 549 amino acid nuclear protein belonging to the Krüppel C2H2-type zinc finger protein family. ZNF266 has one KRAB domain and fourteen C2H2 zinc fingers. Due to the presence of these domains, ZNF266 is thought to be involved in transcriptional regulation. Repression of ZNF266 results in the blocking of erythroid differentiation and partial blocking of megakaryocytic differentiation, possibly indicating a role in the differentiation of erythroids and megakaryocytes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2509R-CY7)
Fournisseur:
Bioss
Description:
Required for assembly and stability of the aminoacyl-tRNA synthase complex. Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2374R-PE)
Fournisseur:
Bioss
Description:
TAP is an integral transmembrane protein involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. It is a heterodimer of TAP1 and TAP2, and the peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. TAP is inducible by interferon gamma and belongs to the ABC transporter family, MDR subfamily. TAP also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. TAP is inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. It is inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP and prevents the conformational rearrangement of TAP induced by peptide binding.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2374R-A350)
Fournisseur:
Bioss
Description:
TAP is an integral transmembrane protein involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. It is a heterodimer of TAP1 and TAP2, and the peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. TAP is inducible by interferon gamma and belongs to the ABC transporter family, MDR subfamily. TAP also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. TAP is inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. It is inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP and prevents the conformational rearrangement of TAP induced by peptide binding.
UOM:
1 * 100 µl
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
