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Catalog Number: (10342-266)
Supplier: Bioss
Description: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity).


Catalog Number: (10748-618)
Supplier: Prosci
Description: Cyclin O Antibody: Cyclin O, also known as CCNO, has recently been identified as a Cdk1- and Cdk2-activating cyclin specific to apoptosis in lymphoid cells. Cyclin O binds to and activates Cdk2 in response to instrinsic apoptotic stimuli such as glucocorticoids or DNA-damaging agents. Supression of Cyclin O expression by shRNA leads to the inhibition of glucocorticoid and DNA-damage-induced apoptosis due to a failure of apical caspase activation while leaving the CD95 death receptor-mediated apoptosis intact. Note: this gene, which had a previous symbol of UNG2, was erroneously identified as a uracil DNA glycosylase. A later publication identified this gene's product as a cyclin protein family member.


Catalog Number: (76085-408)
Supplier: Bioss
Description: Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. In vein endothelial cells, inhibits PI3K/Akt signaling activity and thus induces apoptosis in response to the oxidant peroxynitrite (in vitro). Regulates UV radiation-induced DNA damage response mediated by CDKN1A.


Catalog Number: (10454-352)
Supplier: Bioss
Description: DRAK1 (DAP kinase-related apoptosis-inducing protein kinase 1) is a novel member of the ser/thr protein kinase family, which mediate apoptosis through their catalytic activities. The full-length cDNA encodes a deduced 414-amino acid protein with a molecular mass of 46.56 kD. DRAKs contain an N-terminal kinase domain and a C-terminal regulation domain. DRAK1 messenger RNA appears to be ubiquitously expressed in human tissues. Overexpression of DRAK1 induces apoptosis. It has been shown in vitro that DRAK1 is capable of autophosphorylation and of phosphorylating the myosin light chain as an exogenous substrate, and that the noncatalytic C terminus is crucial for full kinase activity.


Catalog Number: (10801-050)
Supplier: Rockland Immunochemical
Description: Cyclin O, also known as CCNO, has recently been identified as a Cdk1- and Cdk2-activating cyclin specific to apoptosis in lymphoid cells. Cyclin O binds to and activates Cdk2 in response to instrinsic apoptotic stimuli such as glucocorticoids or DNA-damaging agents. Supression of Cyclin O expression by shRNA leads to the inhibition of glucocorticoid and DNA-damage-induced apoptosis due to a failure of apical caspase activation while leaving the CD95 death receptor-mediated apoptosis intact. Note: this gene, which had a previous symbol of UNG2, was erroneously identified as a uracil DNA glycosylase. A later publication identified this gene's product as a cyclin protein family member.


Catalog Number: (10454-142)
Supplier: Bioss
Description: DRAK1 (DAP kinase-related apoptosis-inducing protein kinase 1) is a novel member of the ser/thr protein kinase family, which mediate apoptosis through their catalytic activities. The full-length cDNA encodes a deduced 414-amino acid protein with a molecular mass of 46.56 kD. DRAKs contain an N-terminal kinase domain and a C-terminal regulation domain. DRAK1 messenger RNA appears to be ubiquitously expressed in human tissues. Overexpression of DRAK1 induces apoptosis. It has been shown in vitro that DRAK1 is capable of autophosphorylation and of phosphorylating the myosin light chain as an exogenous substrate, and that the noncatalytic C terminus is crucial for full kinase activity.


Catalog Number: (76119-572)
Supplier: Bioss
Description: TID1 is a human homolog of the Drosophila tumor suppressor lethal tumerous imaginal discs and encodes two mitochondrial matrix localized splice variants of human Tid1 designated hTid1S and hTid1L. These proteins are the conserved members of the DnaJ family of proteins which act as cochaperons for mitochondrial Hsp70. They contain a conserved tetrahedrical J domain which binds to Hsp70 chaperones and activates their ATPase activity. Expression of hTid1L increases apoptosis induced by DNA damaging agents as mitomycin C and TNF alpha. A J domain mutant of hTid1L can dominantly suppress apoptosis and in sharp contrast the J domain mutant of hTid1S increases apoptosis. Expression of hTid1S and hTid1L affects cytochrome c release from the mitochondria and caspase 3 activation, while activation of caspase 8 is unaffected. It is strongly suggested that these two splice variants exert their anti and pro apoptotic effects through discrete substrates and activities. Hence the relative abundance of these proteins or their substrates may allow the mitochondria to dampen or enhance the apoptotic signals.


Catalog Number: (76119-574)
Supplier: Bioss
Description: TID1 is a human homolog of the Drosophila tumor suppressor lethal tumerous imaginal discs and encodes two mitochondrial matrix localized splice variants of human Tid1 designated hTid1S and hTid1L. These proteins are the conserved members of the DnaJ family of proteins which act as cochaperons for mitochondrial Hsp70. They contain a conserved tetrahedrical J domain which binds to Hsp70 chaperones and activates their ATPase activity. Expression of hTid1L increases apoptosis induced by DNA damaging agents as mitomycin C and TNF alpha. A J domain mutant of hTid1L can dominantly suppress apoptosis and in sharp contrast the J domain mutant of hTid1S increases apoptosis. Expression of hTid1S and hTid1L affects cytochrome c release from the mitochondria and caspase 3 activation, while activation of caspase 8 is unaffected. It is strongly suggested that these two splice variants exert their anti and pro apoptotic effects through discrete substrates and activities. Hence the relative abundance of these proteins or their substrates may allow the mitochondria to dampen or enhance the apoptotic signals.


Catalog Number: (10231-976)
Supplier: Bioss
Description: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.


Catalog Number: (10800-344)
Supplier: Rockland Immunochemical
Description: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells and is caused by caspase activation. Proteins that comprise the Bcl-2 family appear to control the activation of these enzymes. One such member is multi-domain antiapoptotic protein Bfl-1, which is overexpressed in stomach and other cancers. Bfl-1 can interact with Bax and suppress apoptosis by inhibiting the release of cytochrome c and caspase-3 activation. It is upregulated in cisplatin-resistant human bladder tumors, suggesting that its expression may be important for cisplatin resistance and inhibition of apoptosis in cancer cells. At least two isoforms of Bfl-1 are known to exist.


Catalog Number: (10749-266)
Supplier: Prosci
Description: Apaf1 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. The mammalian homologous of the key cell death gene CED-4 in C. elegans was 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. Apaf1 can also associate with caspase-4 and caspase-8. Apaf1 transcript is ubiquitously expressed in human tissues.


Catalog Number: (10749-388)
Supplier: Prosci
Description: RIP3 Antibody: Certain serine/threonine protein kinases, such as ASK1, RIP, DAP, and ZIP kinases, are mediators of apoptosis. Receptor interacting proteins including RIP and RIP2/RICK mediate apoptosis induced by TNFR1 and Fas, two prototype members in the death receptor family. A novel member in the RIP kinase family was recently identified and designated RIP3. RIP3 contains N-terminal kinase domain but, unlike RIP or RIP2, lacks the C-terminal death or CARD domain. RIP3 binds to RIP and TNFR1, mediates TNFR1 induced apoptosis, and attenuates RIP and TNFR1 induced NF-kappa B activation. Overexpression of RIP3 induces apoptosis and NF-kappa B activation. The messenger RNA of RIP3 is expressed in a subset of adult tissues.


Catalog Number: (75930-232)
Supplier: Rockland Immunochemical
Description: NALP proteins include the apoptosis regulator APAF1 (apoptotic protease activating factor 1) and mammalian NOD-LRR proteins and are thought to be involved in inflammation and reproduction. NALP5, also known as MATER, is a maternal gene required for early embryonic development in mice. Increased NALP5 expression was observed in two neuronal injury models, and transient expression of recombinant NALP5 in neurons induced caspase-3 activation and apoptosis, suggesting that NALP5 also plays a role in caspase activation and apoptosis in injured neurons, and may thus represent a novel target for therapeutic treatment in neurodegenerative disorders.


Catalog Number: (89361-238)
Supplier: Genetex
Description: Apoptosis can be inhibited by a group of proteins called inhibitors of apoptosis (IAPs). These proteins contain a BIR (baculovirus IAP repeat) domain near the amino-terminus. The BIR domain can bind some caspases. Many members of the IAP family of proteins block proteolytic activation of caspase-3 and ~7. For example, XIAP, cIAP 1 and cIAP 2 appear to block cytochrome c-induced activation of caspase-9, thereby preventing initiation of the caspase cascade. Since cIAP 1 and cIAP 2 were first identified as components in the cytosolic death domain-induced complex associated with the TNF family of receptors, they may inhibit apoptosis by additional mechanisms.


Catalog Number: (10411-480)
Supplier: Bioss
Description: Caspase-6 is involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death. Subunit is compose of heterodimer of a18 kDa (p18) and a 11 kDa (p11) subunit. Subcellular location at cytoplasmic. Cleavages by CPP32, caspase-8 or -10 generate the two active subunits. It belongs to the peptidase C14 family.


Catalog Number: (76084-760)
Supplier: Bioss
Description: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seem to have to effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis.


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