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Catalog Number: (89416-542)
Supplier: Prosci
Description: EVER1 Antibody: Epidermodysplasia verruciformis (EV) is an autosomal recessive dermatosis characterized by abnormal susceptibility to human papillomaviruses (HPVs) and a high rate of progression to squamous cell carcinoma on sun-exposed skin. EV is caused by mutations in either of two adjacent genes, EVER1 and EVER2, located on chromosome 17q25.3. Both of these genes encode integral membrane proteins that localize to the endoplasmic reticulum and are predicted to form transmembrane channels. Both EVER1 and EVER2 are members of the transmembrane channel-like (TMC) protein family. EVER1 possesses eight trans-membrane domains and two leucine zipper motifs. EVER1 and EVER2 form a complex and interact with the zinc transporter 1 (ZnT-1), suggesting that EVER1 and EVER2 act to regulate cellular zinc balance.


Catalog Number: (89416-540)
Supplier: Prosci
Description: EVER1 Antibody: Epidermodysplasia verruciformis (EV) is an autosomal recessive dermatosis characterized by abnormal susceptibility to human papillomaviruses (HPVs) and a high rate of progression to squamous cell carcinoma on sun-exposed skin. EV is caused by mutations in either of two adjacent genes, EVER1 and EVER2, located on chromosome 17q25.3. Both of these genes encode integral membrane proteins that localize to the endoplasmic reticulum and are predicted to form transmembrane channels. Both EVER1 and EVER2 are members of the transmembrane channel-like (TMC) protein family. EVER1 possesses eight trans-membrane domains and two leucine zipper motifs. EVER1 and EVER2 form a complex and interact with the zinc transporter 1 (ZnT-1), suggesting that EVER1 and EVER2 act to regulate cellular zinc balance.


Catalog Number: (ABCA_AB120878-5MG)
Supplier: Abcam
Description: 4-OXO-2-NONENAL (4-ONE), T AB120878-5MG

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Catalog Number: (10373-544)
Supplier: Bioss
Description: Pin1 is a Peptidyl-prolyl isomerases (PPIase). Peptidyl-prolyl isomerases (PPIase) facilitate the cis-trans interconversion of the peptidyl-prolyl bond thereby affecting protein folding. Pin1 is a PPIase which specifically recognizes phosphorylated S/T-P bonds. Pin1 has been implicated in tau pathologies that underlie Alzheimer's Disease. Pin1 binds to tau phosphorylated specifically on the Thr231-Pro site and induces conformational changes in tau. Such conformational changes can directly restore the ability of phosphorylated Tau to bind microtubules and promote microtubule assembly and/or facilitate tau dephosphorylation. Pin1 expression inversely correlates with the predicted neuronal vulnerability in normally aged brain and also with actual neurofibrillary degeneration in AD brain. Pin1 could be pivotal for maintainance of normal neuronal function and preventing age-dependent neurodegeneration.


Catalog Number: (75789-290)
Supplier: Prosci
Description: Cytotoxic and Regulatory T-Cell Molecule (CRTAM) is a member of Nectin family under the immunoglobulin superfamily that is expressed by activated CD8+ and NK T cells. CRTAM is found in spleen, thymus, small intestine, peripheral blood, and it is highly expressed by Purkinje cells of the cerebellum. CRTAM is a type I transmembrane glycoprotein containing one Ig-like C2-type domain and one Ig-like V-type domain in its extracellular domain, while its cytoplasmic region shows a potential class I PDZ domain. CRTAM is expressed as a homodimer on the cell surface but does not show homotypic binding in trans. The high affinity of CRTAM/IGSF4 adhesion allows CRTAM to disrupt IGSF4 homotypic interactions. IGSF4 and T cell receptor coengagement of CD8+ cells expressiong CRTAM induces increased IFN gamma or IL-22 production.


Catalog Number: (10797-852)
Supplier: Prosci
Description: Poliovirus receptor-related protein 1 (PVRL1) is also known as Herpes virus entry mediator C (HveC), Herpesvirus Ig-like receptor (HIgR), Nectin-1, CD antigen CD111, PVRL1 / Nectin-1 / CD111 belongs to the nectin family. PVRL1 / Nectin-1 is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate Ca2+-independent cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM). PVRL1 is adhesion molecule found in a wide range of tissues. PVRL1 / Nectin-1 promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between PVRL1/nectin-1 and PVRL3/nectin-3 and between PVRL1/nectin-1 and PVRL4/nectin-4.


Catalog Number: (10100-820)
Supplier: Prosci
Description: NOTCH4 is a member of the Notch family. Members of this Type 1 transmembrane protein family share structural characteristics including an extracellular domain consisting of multiple epidermal growth factor-like (EGF) repeats, and an intracellular domain consisting of multiple, different domain types. Notch family members play a role in a variety of developmental processes by controlling cell fate decisions. The Notch signaling network is an evolutionarily conserved intercellular signaling pathway which regulates interactions between physically adjacent cells. NOTCH4 is cleaved in the trans-Golgi network, and presented on the cell surface as a heterodimer. NOTCH4 functions as a receptor for membrane bound ligands, and may play a role in vascular, renal and hepatic development. NOTCH4 gene may be associated with susceptibility to schizophrenia in a small portion of cases.


Catalog Number: (10094-274)
Supplier: Proteintech
Description: Selenium (Se) is an essential trace element required for the biosynthesis of selenoproteins, and selenocysteine insertion sequence (SECIS) binding protein 2 (SECISBP2, or SBP2) represents a key trans-acting factor for the cotranslational insertion of selenocysteine into selenoproteins. Defects in SBP2 are a cause of abnormal thyroid hormone metabolism (ATHYHM) associated with a reduction in type II iodothyronine deiodinase activity. Mutations in this gene have been associated with a reduction in activity of a specific thyroxine deiodinase, a selenocysteine-containing enzyme, and abnormal thyroid hormone metabolism. Cells depleted of SBP2 have increased levels of ROS, which lead to cellular oxidative stress manifested as DNA lesions, stress granules, and lipid peroxidation, induction of caspase- and cytochrome c-dependent apoptosis, indicating that SBP2 is required for protection against ROS-induced cellular damage and cell survival.


Catalog Number: (10375-016)
Supplier: Bioss
Description: Pin1 is a Peptidyl-prolyl isomerases (PPIase). Peptidyl-prolyl isomerases (PPIase) facilitate the cis-trans interconversion of the peptidyl-prolyl bond thereby affecting protein folding. Pin1 is a PPIase which specifically recognizes phosphorylated S/T-P bonds. Pin1 has been implicated in tau pathologies that underlie Alzheimer's Disease. Pin1 binds to tau phosphorylated specifically on the Thr231-Pro site and induces conformational changes in tau. Such conformational changes can directly restore the ability of phosphorylated Tau to bind microtubules and promote microtubule assembly and/or facilitate tau dephosphorylation. Pin1 expression inversely correlates with the predicted neuronal vulnerability in normally aged brain and also with actual neurofibrillary degeneration in AD brain. Pin1 could be pivotal for maintainance of normal neuronal function and preventing age-dependent neurodegeneration.


Catalog Number: (10373-538)
Supplier: Bioss
Description: Pin1 is a Peptidyl-prolyl isomerases (PPIase). Peptidyl-prolyl isomerases (PPIase) facilitate the cis-trans interconversion of the peptidyl-prolyl bond thereby affecting protein folding. Pin1 is a PPIase which specifically recognizes phosphorylated S/T-P bonds. Pin1 has been implicated in tau pathologies that underlie Alzheimer's Disease. Pin1 binds to tau phosphorylated specifically on the Thr231-Pro site and induces conformational changes in tau. Such conformational changes can directly restore the ability of phosphorylated Tau to bind microtubules and promote microtubule assembly and/or facilitate tau dephosphorylation. Pin1 expression inversely correlates with the predicted neuronal vulnerability in normally aged brain and also with actual neurofibrillary degeneration in AD brain. Pin1 could be pivotal for maintainance of normal neuronal function and preventing age-dependent neurodegeneration.


Catalog Number: (10082-968)
Supplier: Proteintech
Description: AP3B1 is the 140-kDa β3A subunit of the adaptor-related protein complex-3 (AP-3), a ubiquitous heterotetrameric complex that is localized to the trans-Golgi network and endosomes and is involved in protein trafficking to lysosomes or specialized endosomal-lysosomal organelles . This complex is composed of two lager subunits (δ and β3A or β3B), a medium subunit (μ3A or μ3B), and a small subunit (σ3A or σ3B). The absence of the β3A subunit (AP3B1) results in the loss of stability of AP3 and leads to degradation of μ3A, to which β3A is directly bound, while the other subunits are variably affected . AP3B1 contains three main domains: the N-terminal head domain, the hinge, and the C-terminal ear domain. It has been reported as a target of IP(7)-mediated pyrophosphorylation . Defects in AP3B1 are the cause of Hermansky-Pudlak syndrome type 2 (HPS2) .


Catalog Number: (75923-872)
Supplier: Biotium
Description: Cytochrome c is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic Cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, Cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of Cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of Cytochrome c and to induce cell death. The release of Cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a Cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.


Supplier: Biotium
Description: Cytochrome c is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic Cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, Cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of Cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of Cytochrome c and to induce cell death. The release of Cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a Cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.

Catalog Number: (10085-306)
Supplier: Proteintech
Description: CTH, also named as Gamma-cystathionase and CSE, belongs to the trans-sulfuration enzymes family. It catalyzes the last step in the transsulfuration pathway from methionine to cysteine. CTH has broad substrate specificity. It converts cystathionine to cysteine, ammonia and 2-oxobutanoate. And it converts two cysteine molecules to lanthionine and hydrogen sulfide. CTH can also accept homocysteine as substrate. It specificity depends on the levels of the endogenous substrates. It generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. The CSE/H2S pathway is upregulated in the heart in a murine model of CVB3-induced myocarditis and that inhibition of endogenous H2S is beneficial to treatment early in the disease while administration of exogenous H2S is protective to infected myocardium during the later stage. Defects in CTH are the cause of cystathioninuria.


Supplier: Biotium
Description: Cytochrome c is a well-characterized mobile electron transport protein that is essential to energy conversion in all aerobic organisms. In mammalian cells, this highly conserved protein is normally localized to the mitochondrial inter-membrane space. More recent studies have identified cytosolic Cytochrome c as a factor necessary for activation of apoptosis. During apoptosis, Cytochrome c is trans-located from the mitochondrial membrane to the cytosol, where it is required for activation of caspase-3 (CPP32). Overexpression of Bcl-2 has been shown to prevent the translocation of Cytochrome c, thereby blocking the apoptotic process. Overexpression of Bax has been shown to induce the release of Cytochrome c and to induce cell death. The release of Cytochrome c from the mitochondria is thought to trigger an apoptotic cascade, whereby Apaf-1 binds to Apaf-3 (caspase-9) in a Cytochrome c-dependent manner, leading to caspase-9 cleavage of caspase-3.

Catalog Number: (10423-850)
Supplier: Bioss
Description: Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.


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