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Supplier: Biotium
Description: This antibody 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: 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.

Catalog Number: (10408-978)
Supplier: Bioss
Description: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs).


Supplier: Adipogen
Description: Non-phorbol type tumor promoter. Reversible, potent and selective serine threonine protein phosphatase inhibitor. PP2A (IC50=0.2-1nM), PP1 (IC50=3-15nM), PP2B (IC50= >1µM). Does not inhibit PP2C. Stimulates intracellular protein phosphorylation. Useful tool for studying cellular processes that are regulated by phosphorylation. Does not affect activity of acid phosphatase, alkaline phosphatase and tyrosine phosphatase. Mimics the effects of insulin. Activates atypical protein kinase C (zeta/lambda) in 3T3/L1 adipocytes. Enhances transmitter release at neuromuscular junctions. Apoptosis inhibitor. Induces apoptosis in human breast carcinoma cells (MB-231 and MCF-7) and in myeloid cells. Neurotoxic. Used to study various cellular processes including cell cycle, apoptosis, nitric oxide metabolism and calcium signaling. Stimulates cell motility, loss of stabilization of focal adhesions and a consequent loss of cytoskeletal organization.

Supplier: Adipogen
Description: Non-phorbol type tumor promoter. Reversible, potent and selective serine threonine protein phosphatase inhibitor. PP2A (IC50=0.2-1nM), PP1 (IC50=3-15nM), PP2B (IC50=>1µM). Does not inhibit PP2C. Stimulates intracellular protein phosphorylation. Useful tool for studying cellular processes that are regulated by phosphorylation. Does not affect activity of acid phosphatase, alkaline phosphatase and tyrosine phosphatase. Mimics the effects of insulin. Activates atypical protein kinase C (zeta/lambda) in 3T3/L1 adipocytes. Enhances transmitter release at neuromuscular junctions. Apoptosis inhibitor. Induces apoptosis in human breast carcinoma cells (MB-231 and MCF-7) and in myeloid cells. Neurotoxic. Used to study various cellular processes including cell cycle, apoptosis, nitric oxide metabolism and calcium signaling. Stimulates cell motility, loss of stabilization of focal adhesions and a consequent loss of cytoskeletal organization.

Catalog Number: (102987-192)
Supplier: Adipogen
Description: Non-phorbol type tumor promoter. Reversible, potent and selective serine threonine protein phosphatase inhibitor. PP2A (IC50=0.2-1nM), PP1 (IC50=3-15nM), PP2B (IC50=>1µM). Does not inhibit PP2C. Stimulates intracellular protein phosphorylation. Useful tool for studying cellular processes that are regulated by phosphorylation. Does not affect activity of acid phosphatase, alkaline phosphatase and tyrosine phosphatase. Mimics the effects of insulin. Activates atypical protein kinase C (zeta/lambda) in 3T3/L1 adipocytes. Enhances transmitter release at neuromuscular junctions. Apoptosis inhibitor. Induces apoptosis in human breast carcinoma cells (MB-231 and MCF-7) and in myeloid cells. Neurotoxic. Used to study various cellular processes including cell cycle, apoptosis, nitric oxide metabolism and calcium signaling. Stimulates cell motility, loss of stabilization of focal adhesions and a consequent loss of cytoskeletal organization.


Catalog Number: (10417-750)
Supplier: Bioss
Description: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4.


Catalog Number: (10234-236)
Supplier: Bioss
Description: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4.


Catalog Number: (200061-476)
Supplier: Enzo Life Sciences
Description: Osteopontin (OPN) is an acidic extracellular matrix cell adhesion protein that is relatively abundant not only in bone matrix, plasma, urine, and milk, but is also found in malignant and atherogenic tissues. Phosphorylation, glycosylation and calcium modifications allow intact and fragmented Osteopontin to direct a variety of diverse responses including tissue remodeling, inflammation and cell survival. Plasma Osteopontin has been shown to provide prognostic information in breast, prostate, colon, and lung cancers as well as metastatic carcinomas. The notable presence of Osteopontin in a variety of tumors is strongly correlated to pathological stage, suggesting its critical role in tumor invasiveness, progression and metastasis. In addition, Osteopontin inhibits inducible nitric oxide synthase activity, thereby protecting tumor cells from NO-mediated macrophage cytotoxic attack. Osteopontin is found in atherosclerotic plaques and may drive a number of diabetic vascular pathologies.


Catalog Number: (10366-014)
Supplier: Bioss
Description: Syntrophins are cytoplasmic peripheral membrane scaffold proteins that are components of the dystrophin-associated protein complex. This gene is a member of the syntrophin gene family and encodes the most common syntrophin isoform found in cardiac tissues. The N-terminal PDZ domain of this syntrophin protein interacts with the C-terminus of the pore-forming alpha subunit (SCN5A) of the cardiac sodium channel Nav1.5. This protein also associates cardiac sodium channels with the nitric oxide synthase-PMCA4b (plasma membrane Ca-ATPase subtype 4b) complex in cardiomyocytes. This gene is a susceptibility locus for Long-QT syndrome (LQT) - an inherited disorder associated with sudden cardiac death from arrhythmia - and sudden infant death syndrome (SIDS). This protein also associates with dystrophin and dystrophin-related proteins at the neuromuscular junction and alters intracellular calcium ion levels in muscle tissue. [provided by RefSeq, Jan 2013].


Supplier: Biotium
Description: This antibody 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: Adipogen
Description: Non-phorbol type tumor promoter. Reversible, potent and selective serine threonine protein phosphatase inhibitor. PP2A (IC50=0.2-1nM), PP1 (IC50=3-15nM), PP2B (IC50=>1µM). Does not inhibit PP2C. Stimulates intracellular protein phosphorylation. Useful tool for studying cellular processes that are regulated by phosphorylation. Does not affect activity of acid phosphatase, alkaline phosphatase and tyrosine phosphatase. Mimics the effects of insulin. Activates atypical protein kinase C (zeta/lambda) in 3T3/L1 adipocytes. Enhances transmitter release at neuromuscular junctions. Apoptosis inhibitor. Induces apoptosis in human breast carcinoma cells (MB-231 and MCF-7) and in myeloid cells. Neurotoxic. Used to study various cellular processes including cell cycle, apoptosis, nitric oxide metabolism and calcium signaling. Stimulates cell motility, loss of stabilization of focal adhesions and a consequent loss of cytoskeletal organization.

Catalog Number: (10082-084)
Supplier: Proteintech
Description: APEX1, also named as APE, APE1, HAP1 and REF-1, belongs to the DNA repair enzymes AP/ExoA family. It is a multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are in DNA repair and redox regulation of transcriptional factors. APEX nuclease is a DNA repair enzyme having apurinic/apyrimidinic (AP) endonuclease, 3-prime,5-prime-exonuclease, DNA 3-prime repair diesterase, and DNA 3-prime-phosphatase activities. On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. APEX1 is involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). When acetylated at Lys-6 and Lys-7, APEX1 stimulates the YBX1-mediated MDR1 promoter activity, leading to drug resistance. It also acts as an endoribonuclease involved in the control of single-stranded RNA metabolism. It plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, APEX1 plays a role in the rRNA quality control process during cell cycle progression. 10323-1-AP is a rabbit polyclonal antibody raised against a fusion protein corresponding to an internal region of human APEX1.


Catalog Number: (10082-082)
Supplier: Proteintech
Description: APEX1, also named as APE, APE1, HAP1 and REF-1, belongs to the DNA repair enzymes AP/ExoA family. It is a multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are in DNA repair and redox regulation of transcriptional factors. APEX nuclease is a DNA repair enzyme having apurinic/apyrimidinic (AP) endonuclease, 3-prime,5-prime-exonuclease, DNA 3-prime repair diesterase, and DNA 3-prime-phosphatase activities. On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. APEX1 is involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). When acetylated at Lys-6 and Lys-7, APEX1 stimulates the YBX1-mediated MDR1 promoter activity, leading to drug resistance. It also acts as an endoribonuclease involved in the control of single-stranded RNA metabolism. It plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, APEX1 plays a role in the rRNA quality control process during cell cycle progression. 10203-1-AP is a rabbit polyclonal antibody raised against full length APE1 of human origin.


Catalog Number: (10417-730)
Supplier: Bioss
Description: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4.


Catalog Number: (10417-742)
Supplier: Bioss
Description: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4.


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