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block+heaters+
Numéro de catalogue:
(BOSSBS-1049R-A488)
Fournisseur:
Bioss
Description:
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8191R-A647)
Fournisseur:
Bioss
Description:
Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8191R-HRP)
Fournisseur:
Bioss
Description:
Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8191R-A555)
Fournisseur:
Bioss
Description:
Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes.
UOM:
1 * 100 µl
Fournisseur:
ENZO LIFE SCIENCES
Description:
Dehydrins are a family of proteins that become abundant during dessication in seedlings and embryos of cereal crop plants including barley, corn, wheat, and rice. Dehydrin proteins have a highly conserved lysine-rich block (KIKEKLPG) found near the carboxy terminus which appears to be characteristic of, and unique to Dehydrins.
Numéro de catalogue:
(BOSSBS-12215R-CY3)
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-5161R-FITC)
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-A647)
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-6675R-A488)
Fournisseur:
Bioss
Description:
Forms a voltage-independent potassium channel that is activated by intracellular calcium. Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. The channel is blocked by clotrimazole and charybdotoxin but is insensitive to apamin.
UOM:
1 * 100 µl
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:
(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-6625R)
Fournisseur:
Bioss
Description:
Insig2 is highly similar to the protein product encoded by gene Insig1. Both Insig1 protein and Insig2 protein are endoplasmic reticulum proteins that block the processing of sterol regulatory element binding proteins (SREBPs) by binding to SREBP cleavage-activating protein (SCAP), and thus prevent SCAP from escorting SREBPs to the Golgi.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5161R-CY3)
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-CY5.5)
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
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est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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