578 Results for: "trans-4-phenylcyclohexanecarboxylic acid"

Supplier: Thermo Scientific

This antibody is predicted to react with bovine, canine, mouse and rat based on sequence homology. This gene belongs to a group of vacuolar protein sorting genes that, when functionally impaired, disrupt the efficient delivery of vacuolar hydrolases. The protein encoded by this gene is a component of a large multimeric complex, termed the retromer complex, which is involved in retrograde transport of proteins from endosomes to the trans-Golgi network. This VPS protein may be involved in the formation of the inner shell of the retromer coat for retrograde vesicles leaving the prevacuolar compartment. Alternative splice variants encoding different isoforms, and usage of multiple polyadenylation sites have been found for this gene.

Supplier: Thermo Scientific

RB1 likely acts as a regulator of other genes. It forms a complex with adenovirus E1A and with SV40 large T antigen, acts as a tumor suppressor, and may bind and modulate functionally certain cellular proteins with which T and E1A compete for pocket binding. RB1 is a potent inhibitor of E2F-mediated trans-activation, and also recruits and targets histone methyltransferase SUV39H1 leading to epigenetic transcriptional repression. This protein inhibits the intrinsic kinase activity of TAF1. Defects in RB1 are the cause of childhood cancer retinoblastoma (RB), a congenital malignant tumor that arises from the nuclear layers of the retina. Defects in RB1 are also a cause of bladder cancer and osteogenic sarcoma.

Supplier: Proteintech

Complexins are soluble proteins that regulate the activity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes necessary for vesicle fusion. Neuronal specific complexin 1 (CPLX1) has inhibitory and stimulatory effects on exocytosis by clamping trans-SNARE complexes in a prefusion state and promoting conformational changes to facilitate membrane fusion following cell stimulation. Complexin2 (CPLX2) is a pre-synaptic protein believed to regulate neurotransmitter release from pre-synaptic terminals, it is downregulated in schizophrenic patients suffering from depression, animal models of depression and neurological disorders such as Huntington's disease in which depression is a major symptom.

Supplier: Thermo Scientific

This antibody is predicted to react with canine, mouse and rat based on sequence homology. This gene belongs to a group of vacuolar protein sorting genes that, when functionally impaired, disrupt the efficient delivery of vacuolar hydrolases. The protein encoded by this gene is a component of a large multimeric complex, termed the retromer complex, which is involved in retrograde transport of proteins from endosomes to the trans-Golgi network. This VPS protein may be involved in the formation of the inner shell of the retromer coat for retrograde vesicles leaving the prevacuolar compartment. Alternative splice variants encoding different isoforms, and usage of multiple polyadenylation sites have been found for this gene.

Supplier: Prosci

BICD1 Antibody: BICD1 was initially identified as the human homolog to Drosophila Bicaudal-D protein that forms part of the cytoskeleton and mediates the correct sorting of mRNAs for oocyte- and axis-determining factors during oogenesis. BICD1 can bind to dynein-dynactin and co-localizes with Rab6A on the trans-Golgi network and cytoplasmic vesicles, suggesting BICD1 regulates COPI-independent Golgi-ER transport. BICD1 will also interact with Rab6B, a Rab6 isoform that is expressed primarily in brain. Live cell imaging showed bi-directional movement of Rab6B structures in SK-N-SH neurites, indicating that BICD1 is involved in the Rab6B regulation of retrograde cargo transport in neuronal cells.

Supplier: Prosci

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.

Supplier: Prosci

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.

Supplier: Prosci

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.

Supplier: Proteintech

DNA replication licensing factor MCM4 (MCM4), also named Cdc21, acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.This antibody is a rabbit polyclonal antibody raised against the C-terminal 350 aa sequence of MCM4 protein.

Supplier: Proteintech

TP53, also named as P53 and NY-CO-13, belongs to the p53 family that functions as a central mediator for organizing cellresponses to various stress and anticancer drugswith apoptosis,G1- phase arrest, and DNA repair.. In addition, TP53 appears to induce apoptosis through nontranscriptional cytoplasmic processes. In unstressed cells, TP53 is kept inactive essentially through the actions of the ubiquitin ligase MDM2, which inhibits TP53 transcriptional activity and ubiquitinates TP53 to promote its degradation. TP53 acts as a tumor suppressor in many tumor types and induces growth arrest or apoptosis depending on the physiological circumstances and cell type. It is 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.

Supplier: Prosci

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.

Supplier: Proteintech

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: Thermo Scientific

This antibody is predicted to react with mouse and rat based on sequence homology. RB1 likely acts as a regulator of other genes. It forms a complex with adenovirus E1A and with SV40 large T antigen, acts as a tumor suppressor, and may bind and modulate functionally certain cellular proteins with which T and E1A compete for pocket binding. RB1 is a potent inhibitor of E2F-mediated trans-activation, and also recruits and targets histone methyltransferase SUV39H1 leading to epigenetic transcriptional repression. This protein inhibits the intrinsic kinase activity of TAF1. Defects in RB1 are the cause of childhood cancer retinoblastoma (RB), a congenital malignant tumor that arises from the nuclear layers of the retina. Defects in RB1 are also a cause of bladder cancer and osteogenic sarcoma.

Supplier: Proteintech

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) .

Supplier: Proteintech

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.

Supplier: Prosci

GOLPH3 Antibody: GOLPH3 was initially identified as a peripheral membrane protein localized to the trans-Golgi network, but others reported it to be primarily a mitochondrial protein that regulated the mitochondrial mass through the regulation of the mitochondria-specific phospholipid cardiolipin. GOLPH3 has since been implicated in the target of rapamycin (TOR) signalling pathway. Its overexpression in transfected cells led to and increase in anchorage-independent growth and cell proliferation in vitro. Furthermore, GOLPH3-transfected cells enhanced S6 Kinase activity in response to growth factor stimulation by EGF. Simultaneously, AKT phosphorylation increased in these cells, while these events were abrogated in GOLPH3 siRNA treated cells compared to control cells, indicating the GOLPH3 can enhance signalling through TOR-associated complexes. These results suggest that GOLPH3 is a bona fide oncogene and may be a useful target for therapeutic strategies.

Supplier: Proteintech

VPS35 protein belongs to a group of vacuolar protein sorting (VPS) proteins, which ensure the proper delivery of organelle-specific proteins in eukaryotic cells. VPS35 is the core of a multimeric complex, termed the retromer complex, which is involved in retrograde transport of proteins from endosomes to the trans-Golgi network. Vps35 serves as the core of the multimeric complex by binding directly to Vps26 and Vps29 and SNX1. Northern blot analyses in 16 tissues showed that one transcript of Vps35 with a size of 3.6 kb was highly expressed in brain, heart, testis, ovary, small intestine, spleen, skeletal muscle, and placenta and expressed at moderate or low levels in other tissues. Another transcript of Vps35, a message of 3.0 kb, was also expressed with proportionally lower levels than the 3.6-kb transcript in all the tissues except that the 3.0-kb transcript was not detected in brain. Human Vps35 is mapped at 16q13-q21.

Supplier: Prosci

GOLPH3 Antibody: GOLPH3 was initially identified as a peripheral membrane protein localized to the trans-Golgi network, but others reported it to be primarily a mitochondrial protein that regulated the mitochondrial mass through the regulation of the mitochondria-specific phospholipid cardiolipin. GOLPH3 has since been implicated in the target of rapamycin (TOR) signalling pathway. Its overexpression in transfected cells led to and increase in anchorage-independent growth and cell proliferation in vitro. Furthermore, GOLPH3-transfected cells enhanced S6 Kinase activity in response to growth factor stimulation by EGF. Simultaneously, AKT phosphorylation increased in these cells, while these events were abrogated in GOLPH3 siRNA treated cells compared to control cells, indicating the GOLPH3 can enhance signalling through TOR-associated complexes. These results suggest that GOLPH3 is a bona fide oncogene and may be a useful target for therapeutic strategies.

Supplier: Prosci

Notch is synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase (S1 cleavage) in the trans-golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved (S2 cleavage) by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin-dependent gamma-secretase (S3 cleavage) to release the intracellular domain (NICD) from the membrane. Notch functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBP-J kappa and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs.

Supplier: Proteintech

Cadherins are a family of transmembrane glycoproteins that mediate calcium-dependent cell-cell adhesion and play an important role in the maintenance of normal tissue architecture. E-cadherin (epithelial cadherin), also known as CDH1 (cadherin 1) or CAM 120/80, is a classical member of the cadherin superfamily which also include N-, P-, R-, and B-cadherins. It has been regarded as a marker for spermatogonial stem cells in mice. E-cadherin is expressed on the cell surface in most epithelial tissues. The extracellular region of E-cadherin establishes calcium-dependent homophilic trans binding, providing specific interaction with adjacent cells, while the cytoplasmic domain is connected to the actin cytoskeleton through the interaction with p120-, α-, β-, and γ-catenin (plakoglobin). E-cadherin is important in the maintenance of the epithelial integrity, and is involved in mechanisms regulating proliferation, differentiation, and survival of epithelial cell. E-cadherin may also play a role in tumorigenesis. It is considered to be an invasion suppressor protein and its loss is an indicator of high tumor aggressiveness. E-cadherin is sensitive to trypsin digestion in the absence of Ca2+. This polyclonal antibody recognizes 120-kDa intact E-cadherin and its 80-kDa trypsin-cleaved fragment.

Supplier: Thermo Scientific

This antibody is predicted to react with mouse based on sequence homology. TIP47 (tail-interacting protein 47) is a member of PAT family of proteins (perilipin, ADRP, S3-12 and OXPAT) which plays a key role in the packaging/storage of neutral lipids and is required for mannose 6-phosphate receptors (M6PR) transport from endosomes to trans-Golgi network (TGN). TIP47 localizes in cytoplasm, endosome membrane as peripheral membrane protein towards cytoplasmic side, core of lipid bodies/ lipid droplet, in lipid sails and in the envelope, and it interacts with M6PR, IGF2R etc. via the cytoplasmic domain. As a cargo protein, TIP47 facilitates the delivery of M6PR from endosomes to TGN where it binds to cytoplasmic domains of cation-independent/-dependent M6PR and translocates to late endosomes by binding to Rab9 GTPase. Like other PAT family members, TIP47 associates with lipid droplets and influence insulin signaling as evidenced by combined knockout of ADRP /TIP47 leading to decreased insulin sensitivity. During HIV-1 infection, TIP47 acts as a cellular cofactor playing a part in Env incorporation, allowing the encounter and physical association between HIV-1 Gag and Env proteins during viral assembly process. TIP47 is identical to pregnancy-related placental tissue protein 17b (PP17b) and is overexpressed in cervical carcinoma patients wherein it is considered a serum tumor marker.

Supplier: Thermo Scientific Chemicals

trans-2-Butenyl acetate 95%

Supplier: Thermo Scientific Chemicals

Potassium trans-β-styryltrifluoroborate 98%

Supplier: Thermo Scientific Chemicals

Methyl trans-2-hexenoate 98%

Supplier: MilliporeSigma

E-64 Protease Inhibitor

Supplier: Thermo Scientific Chemicals

Elaidic acid 98%

Supplier: Thermo Scientific Chemicals

Ethyl-3-phenylglycidate (mixture of cis and trans isomers) 90+%

Supplier: Thermo Scientific Chemicals

Triethyl-4-phosphonocrotonate cis- and trans-mixture 94%

Supplier: TCI America

CAS Number: 3399-22-2
MDL Number: MFCD00063917
Molecular Formula: C10H16O4
Molecular Weight: 200.23
Purity/Analysis Method: >96.0% (GC)
Form: Crystal
Boiling point (°C): 140
Melting point (°C): 69

Supplier: Thermo Scientific Chemicals

Ethyl-3-benzoylacrylate predominantly trans 94%