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Supplier: Merck
Description: Employed in the synthesis of the first example of a mixed-valence ammonium iron phosphate, NH₄Fe₂(PO₄)₂.

Catalog Number: (ENZOADIKAPNO020F)
Supplier: ENZO LIFE SCIENCES
Description: The diffusible free radical gas nitric oxide (NO) affects a variety of physiological functions, and is a key regulator of the cardiovascular, nervous, and immune systems. NO is synthesized in many tissues from L-arginine, oxygen, and NADPH by three known isoforms of a heme-containing flavoprotein termed NO synthase (nNOS/NOS-I, iNOS/NOS-II, and eNOS/NOS-III). nNOS is a constitutively expressed neuronal NOS isoform that exits in its latent form until it is activated by the binding of calmodulin follo wing elevation of intracellular calcium levels. The C-terminus of nNOS contains a conserved serine residue, Ser1417, analogous to Ser1177 of the constitutively expressed endothelial NOS isoform (eNOS). Phosphorylation of Ser1417 is believed to regulate nNOS activation, particularly in glucose-sensing neurons, where inhibition of AMPK pathways by glucose and leptin serve to suppress nNOS activity, whereas activation of AMPK by insulin leads to nNOS activation.
UOM: 1 * 200 µG

New Product


Supplier: Biotium
Description: Recognizes a protein of 33-55 kDa, identified as CD53 (Workshop V; Code CD53.1). CD53 is expressed on monocytes, and macrophages, granulocytes, dendritic cells, osteoblasts and osteoclasts, NK cells, and on T- and B-cells from every stage of differentiation but is absent from platelets, erythrocytes, and non-haemopoietic cells. CD53 is a member of a family of tetraspan transmembrane proteins, including CD9, CD37, CD63, CD81, and CD82. It associates with integrins, MHC class II molecules, and a tyrosine phosphatase and plays a role in cellular activation as part of a signal transduction complex involving other membrane glycoproteins. Defects of CD53 expression on neutrophils appear to be related with recurrent infectious diseases. Cross-linking CD53 using CD53 antibodies led to cytoplasmic calcium fluxes in B cells, monocytes, and granulocytes and activation of the monocyte oxidative burst.

Supplier: Biotium
Description: Recognizes a protein of 33-55 kDa, identified as CD53 (Workshop V; Code CD53.1). CD53 is expressed on monocytes, and macrophages, granulocytes, dendritic cells, osteoblasts and osteoclasts, NK cells, and on T- and B-cells from every stage of differentiation but is absent from platelets, erythrocytes, and non-haemopoietic cells. CD53 is a member of a family of tetraspan transmembrane proteins, including CD9, CD37, CD63, CD81, and CD82. It associates with integrins, MHC class II molecules, and a tyrosine phosphatase and plays a role in cellular activation as part of a signal transduction complex involving other membrane glycoproteins. Defects of CD53 expression on neutrophils appear to be related with recurrent infectious diseases. Cross-linking CD53 using CD53 antibodies led to cytoplasmic calcium fluxes in B cells, monocytes, and granulocytes and activation of the monocyte oxidative burst.

Supplier: Biotium
Description: Recognizes a protein of 33-55 kDa, identified as CD53 (Workshop V; Code CD53.1). CD53 is expressed on monocytes, and macrophages, granulocytes, dendritic cells, osteoblasts and osteoclasts, NK cells, and on T- and B-cells from every stage of differentiation but is absent from platelets, erythrocytes, and non-haemopoietic cells. CD53 is a member of a family of tetraspan transmembrane proteins, including CD9, CD37, CD63, CD81, and CD82. It associates with integrins, MHC class II molecules, and a tyrosine phosphatase and plays a role in cellular activation as part of a signal transduction complex involving other membrane glycoproteins. Defects of CD53 expression on neutrophils appear to be related with recurrent infectious diseases. Cross-linking CD53 using CD53 antibodies led to cytoplasmic calcium fluxes in B cells, monocytes, and granulocytes and activation of the monocyte oxidative burst.

Catalog Number: (SIAL700312-5ML)
Supplier: Merck
Description: It contains <1.0% oleic acid stabilizing ligands.
UOM: 1 * 5 mL


Supplier: Merck
Description: Iron(II,III) oxide, Sigma-Aldrich®

Catalog Number: (ROTH9348.1)
Supplier: Roth Carl
Description: Zinc oxide
UOM: 1 * 1 kg


Supplier: Roth Carl
Description: Zinc oxide

Catalog Number: (ENZOALX804213R100)
Supplier: ENZO LIFE SCIENCES
Description: Mammalian apurinic/apyrimidinic (AP) endonuclease (APE1; APEX; HAP1; Ref-1) is a multifunctional, bipartite enzyme that belongs to the class II AP endonucleases and that plays an important role in numerous, cellular functions, like repairing abasic sites (loss of purine or pyrimidine base) in DNA, regulating the redox state of other proteins that play roles in oxidative signalling, transcription factor regulation (Fos, Jun, NF-κ B, Myb, HIF-1α, CREB, Pac), cell cycle control (p53) and apoptosis. APE1 initiates the DNA base excision repair (BER) by cleaving the DNA immediately adjacent to the 5’ of an AP site to produce a hydroxyl group at the 3’ terminus of an unmodified nucleotide upstream of the nick and a 5’-deoxyribose phosphate moiety downstream. The product of APE1 is further processed by DNA polymerase β to release 5’-deoxyribose phosphate with its intrinsic lyase activity. The nicked DNA is then sealed by DNA ligase I or DNA ligaseIII/XRCC1 to complete this repair process. In addition to the AP endonuclease activity, APE1 also possesses a 3’-5’ DNA exonuclease activity, a 3’-phosphodiesterase activity, a 3’-phosphatase activity, and a RNase H activity. It has been shown that APE1 is capable of excision L-configuration deoxyribonucleoside analogs from the 3’ termini of DNA. Human APE1 gene is located on chromosome 14q 11.2-12.
UOM: 1 * 100 µl

New Product


Supplier: Merck
Description: Zinc oxide, Sigma-Aldrich®

Supplier: Merck
Description: Cadmium oxide, Sigma-Aldrich®

Supplier: Thermo Fisher Scientific
Description: Zinc oxide ≥99.0% ACS
Catalog Number: (BOSSBS-1687R-CY3)
Supplier: Bioss
Description: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3. Acts as a signaling amplifier of NMDA receptors at extrasynaptic sites for mediating brain damage in stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex and it phosphorylates GRINB at Ser-133 inducing injurious Ca(2+) influx through NMDA receptor channels, resulting in an irreversible neuronal death. Required together with DAPK3 for phosphorylation of RPL13A upon interferon-gamma activation which is causing RPL13A involvement in transcript-selective translation inhibition. Isoform 2 cannot induce apoptosis but can induce membrane blebbing.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1687R-A647)
Supplier: Bioss
Description: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Regulates both type I apoptotic and type II autophagic cell deaths signal, depending on the cellular setting. The former is caspase-dependent, while the latter is caspase-independent and is characterized by the accumulation of autophagic vesicles. Phosphorylates PIN1 resulting in inhibition of its catalytic activity, nuclear localization, and cellular function. Phosphorylates TPM1, enhancing stress fiber formation in endothelial cells. Phosphorylates STX1A and significantly decreases its binding to STXBP1. Phosphorylates PRKD1 and regulates JNK signaling by binding and activating PRKD1 under oxidative stress. Phosphorylates BECN1, reducing its interaction with BCL2 and BCL2L1 and promoting the induction of autophagy. Phosphorylates TSC2, disrupting the TSC1-TSC2 complex and stimulating mTORC1 activity in a growth factor-dependent pathway. Phosphorylates RPS6, MYL9 and DAPK3. Acts as a signaling amplifier of NMDA receptors at extrasynaptic sites for mediating brain damage in stroke. Cerebral ischemia recruits DAPK1 into the NMDA receptor complex and it phosphorylates GRINB at Ser-133 inducing injurious Ca(2+) influx through NMDA receptor channels, resulting in an irreversible neuronal death. Required together with DAPK3 for phosphorylation of RPL13A upon interferon-gamma activation which is causing RPL13A involvement in transcript-selective translation inhibition. Isoform 2 cannot induce apoptosis but can induce membrane blebbing.
UOM: 1 * 100 µl


Supplier: BUCHI
Description: Tubing, silicone, 6/9 mm, 1 m, transparent, For: Büchi Rotavapor® R-210 / R-215

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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 at +43 1 97002 - 0.
Dual use goods can only be delivered within the European Union.
Dual use goods can only be delivered within the European Union.
This product has been blocked by your organization. Please contact your purchasing department for more information.
The original product is no longer available. The replacement shown is available.
This product is no longer available. Alternatives may be available by searching with the VWR Catalog Number listed above. If you need further assistance, please call VWR Customer Service at +43 1 97002 - 0.
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