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#28878979   2017/09/07 Save this To Up

Oriented, molecularly imprinted cavities with dual binding sites for highly sensitive and selective recognition of cortisol.

Novel, molecularly imprinted polymers (MIPs) were developed for the highly sensitive and selective recognition of the stress marker cortisol. Oriented, homogeneous cavities with two binding sites for cortisol were fabricated by surface-initiated atom transfer radical polymerization, using a cortisol motif template molecule (TM1) which consists of a polymerizable moiety attached at the 3-carbonyl group of cortisol via an oxime linkage and an adamantane carboxylate moiety coupled with the 21-hydroxyl group. TM1 was orientationally immobilized on a β-cyclodextrin (β-CD)-grafted gold-coated sensor chip by inclusion of the adamantane moiety of TM1, followed by copolymerization of a hydrophilic comonomer, 2-methacryloyloxyethyl phosphorylcholine, with or without a cross-linker, N,N'-methylenebisacrylamide. Subsequent cleavage of the oxime linkage leaves the imprinted cavities that contain dual binding sites-namely, the aminooxy group and β-CD-capable of oxime formation and hydrophobic interaction, respectively. As an application, MIP-based picomolar level detection of cortisol was demonstrated by a competitive binding assay using a fluorescent competitor. Cross-linking of the MIP imparts rigidity to the binding cavities, and improves the selectivity and sensitivity significantly, reducing the limit of detection to 4.8 pM. In addition, detection of cortisol in saliva samples was demonstrated as a feasibility study.

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Cortisol Binding Globulin Beta Amyloid (1 42) High Sheep Anti-Human Cortisol Rabbit Anti-Rat Androgen Highly Sensitive 8 OHdG C 8 Octadecyloxypyrene 1,3, 4 Methylumbelliferyl sulf Cellufine Formyl , 50 ml Cellufine Formyl Media Cellufine Formyl , 500 ml Cellufine Formyl Media Cellufine Formyl Media

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#28872857   2017/09/05 Save this To Up

Cross-Linked Collagen Triple Helices by Oxime Ligation.

Covalent cross-links are crucial for the folding and stability of triple-helical collagen, the most abundant protein in nature. Cross-linking is also an attractive strategy for the development of synthetic collagen-based biocompatible materials. Nature uses interchain disulfide bridges to stabilize collagen trimers. However, their implementation into synthetic collagen is difficult and requires the replacement of the canonical amino acids (4R)-hydroxyproline and proline by cysteine or homocysteine, which reduces the preorganization and thereby stability of collagen triple helices. We therefore explored alternative covalent cross-links that allow for connecting triple-helical collagen via proline residues. Here, we present collagen model peptides that are cross-linked by oxime bonds between 4-aminooxyproline (Aop) and 4-oxoacetamidoproline placed in coplanar Xaa and Yaa positions of neighboring strands. The covalently connected strands folded into hyperstable collagen triple helices (Tm ≈ 80 °C). The design of the cross-links was guided by an analysis of the conformational properties of Aop, studies on the stability and functionalization of Aop-containing collagen triple helices, and molecular dynamics simulations. The studies also show that the aminooxy group exerts a stereoelectronic effect comparable to fluorine and introduce oxime ligation as a tool for the functionalization of synthetic collagen.

1827 related Products with: Cross-Linked Collagen Triple Helices by Oxime Ligation.

CL APC (Cross linked Phyc Polystyrene Particle Size Picro-Sirius Red Stain K ELCI ELISA grade chick ty ELCI ELISA grade chick ty ELISA grade chick type I ELBI ELISA grade bovine t ELBI ELISA grade bovine t ELISA grade bovine type I ELISA grade porcine type ELPI ELISA grade porcine ELPI ELISA grade porcine

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#28827125   2017/08/22 Save this To Up

New method for estimating clustering of DNA lesions induced by physical/chemical mutagens using fluorescence anisotropy.

We have developed a new method for estimating the localization of DNA damage such as apurinic/apyrimidinic sites (APs) on DNA using fluorescence anisotropy. This method is aimed at characterizing clustered DNA damage produced by DNA-damaging agents such as ionizing radiation and genotoxic chemicals. A fluorescent probe with an aminooxy group (AlexaFluor488) was used to label APs. We prepared a pUC19 plasmid with APs by heating under acidic conditions as a model for damaged DNA, and subsequently labeled the APs. We found that the observed fluorescence anisotropy (robs) decreases as averaged AP density (λAP: number of APs per base pair) increases due to homo-FRET, and that the APs were randomly distributed. We applied this method to three DNA-damaging agents, (60)Co γ-rays, methyl methanesulfonate (MMS), and neocarzinostatin (NCS). We found that robs-λAP relationships differed significantly between MMS and NCS. At low AP density (λAP < 0.001), the APs induced by MMS seemed to not be closely distributed, whereas those induced by NCS were remarkably clustered. In contrast, the AP clustering induced by (60)Co γ-rays was similar to, but potentially more likely to occur than, random distribution. This simple method can be used to estimate mutagenicity of ionizing radiation and genotoxic chemicals.

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Amplite™ Fluorimetric F QuantiChrom™ Formaldehy QuantiChrom™ Urea Assay 5 Carboxy X Rhodamine, NH OxiSelect™ Cellular UV- MOUSE ANTI APAAP COMPLEX, Cellufine Formyl , 50 ml Cellufine Formyl Media Cellufine Formyl , 500 ml Cellufine Formyl Media Cellufine Formyl Media Protease, DNASE free hea

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#28783731   2017/08/07 Save this To Up

Metabolic control of TH17 and induced Treg cell balance by an epigenetic mechanism.

Metabolism has been shown to integrate with epigenetics and transcription to modulate cell fate and function. Beyond meeting the bioenergetic and biosynthetic demands of T-cell differentiation, whether metabolism might control T-cell fate by an epigenetic mechanism is unclear. Here, through the discovery and mechanistic characterization of a small molecule, (aminooxy)acetic acid, that reprograms the differentiation of T helper 17 (TH17) cells towards induced regulatory T (iTreg) cells, we show that increased transamination, mainly catalysed by GOT1, leads to increased levels of 2-hydroxyglutarate in differentiating TH17 cells. The accumulation of 2-hydroxyglutarate resulted in hypermethylation of the Foxp3 gene locus and inhibited Foxp3 transcription, which is essential for fate determination towards TH17 cells. Inhibition of the conversion of glutamate to α-ketoglutaric acid prevented the production of 2-hydroxyglutarate, reduced methylation of the Foxp3 gene locus, and increased Foxp3 expression. This consequently blocked the differentiation of TH17 cells by antagonizing the function of transcription factor RORγt and promoted polarization into iTreg cells. Selective inhibition of GOT1 with (aminooxy)acetic acid ameliorated experimental autoimmune encephalomyelitis in a therapeutic mouse model by regulating the balance between TH17 and iTreg cells. Targeting a glutamate-dependent metabolic pathway thus represents a new strategy for developing therapeutic agents against TH17-mediated autoimmune diseases.

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Cell Cycle Control Phosph Mouse Anti-Human CD34 Tar EZH2 KMT6 Control Peptid GFP control peptide anti Anti C Reactive Protein A Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl

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#28695504   2017/07/11 Save this To Up

Detecting Protein ADP-Ribosylation Using a Clickable Aminooxy Probe.

ADP-ribosylation, a posttranslational modification catalyzed by a family of enzymes known as poly(ADP-ribose) polymerases (PARPs, 17 in humans), regulates diverse cellular processes. To aid in understanding the functions of ADP-ribosylation in cells, we developed a clickable aminooxy probe, AO-alkyne, which detects ADP-ribosylation of acidic amino acids. AO-alkyne can be used to detect auto-ADP-ribosylation of PARP10 in cells following Cu-catalyzed click conjugation to an azide reporter. This method can be extended to other PARP family members that catalyze ADP-ribosylation on acidic amino acids, providing a convenient and direct readout of PARP activity in cells.

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Anti-ARL1(ADP-ribosylatio Anti ARL1(ADP ribosylatio Anti-ARL5B(ADP-ribosylati Anti ARL5B(ADP ribosylati Anti-ARL6(ADP-ribosylatio Anti ARL6(ADP ribosylatio ADP-ribosylation factor 3 Polyclonal Antibody ADP-R 7-(Diethylamino)coumarin- Anti-ADP Ribosylation Fac Anti ADP Ribosylation Fac Glial Fibrillary Acidic

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#28682060   2017/07/06 Save this To Up

Aminooxylated Carbohydrates: Synthesis and Applications.

Among other classes of biomolecules, carbohydrates and glycoconjugates are widely involved in numerous biological functions. In addition to addressing the related synthetic challenges, glycochemists have invested intense efforts in providing access to structures that can be used to study, activate, or inhibit these biological processes. Over the past few decades, aminooxylated carbohydrates have been found to be key building blocks for achieving these goals. This review provides the first in-depth overview covering several aspects related to the syntheses and applications of aminooxylated carbohydrates. After a brief introduction to oxime bonds and their relative stabilities compared to related C═N functions, synthetic aspects of oxime ligation and methodologies for introducing the aminooxy functionality onto both glycofuranosyls and glycopyranosyls are described. The subsequent section focuses on biological applications involving aminooxylated carbohydrates as components for the construcion of diverse architectures. Mimetics of natural structures represent useful tools for better understanding the features that drive carbohydrate-receptor interaction, their biological output and they also represent interesting structures with improved stability and tunable properties. In the next section, multivalent structures such as glycoclusters and glycodendrimers obtained through oxime ligation are described in terms of synthetic design and their biological applications such as immunomodulators. The second-to-last section discusses miscellaneous applications of oxime-based glycoconjugates, such as enantioselective catalysis and glycosylated oligonucleotides, and conclusions and perspectives are provided in the last section.

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MOUSE ANTI BOVINE ROTAVIR Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650 NATIVE HUMAN PROLACTIN, P BriteRuler™ 1 kb DNA La BriteRuler Prestained Pro AZD-3514 Mechanisms: Andr 17β-Acetoxy-2α-bromo-5 (5α,16β)-N-Acetyl-16-[2

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#28639122   2017/06/22 Save this To Up

Targeting Prostate-Specific Membrane Antigen (PSMA) with F-18-Labeled Compounds: the Influence of Prosthetic Groups on Tumor Uptake and Clearance Profile.

Prostate-specific membrane antigen (PSMA) is an important biomarker expressed in the majority of prostate cancers. The favorable positron emission tomography (PET) imaging profile of the PSMA imaging agent 2-(3-(1-carboxy-5-[(6-[(18)F]fluoro-pyridine-3-carbonyl)-amino]-pentyl)-ureido)-pentane-dioic acid [(18)F]DCFPyL in preclinical prostate cancer models and in prostate cancer patients stimulated the development and validation of other fluorine-containing PSMA inhibitors to further enhance pharmacokinetics and simplify production methods. Here, we describe the synthesis and radiopharmacological evaluation of various F-18-labeled PSMA inhibitors which were prepared through different prosthetic group chemistry strategies.

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Mouse Anti-Prostate Speci PSA (Prostate Specific A PSA (Prostate Specific A PSA (Prostate Specific A PSA (Prostate Specific A PSA (Prostate Specific A PSA (Prostate Specific A Human Prostate Specific A Multiple organ cancer tis Multiple organ tumor tiss Prostate cancer, hyperpla Prostate-Specific Antigen

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#28422167   2017/04/19 Save this To Up

Biotin-transfer from a trifunctional crosslinker for identification of cell surface receptors of soluble protein ligands.

Here we describe a novel crosslinker and its application as a biotin-transfer reagent to identify cell surface receptors of soluble protein ligands on live cells. This crosslinker contains three functional groups: an aldehyde-reactive aminooxy group, a sulfhydryl, and a biotin (ASB). It is readily synthesized via a 3-step addition reaction using standard solid-phase peptide synthesis methods and commercially available intermediates, allowing access to laboratories without specialized synthetic chemistry capabilities. For the biotin-transfer method, ASB is linked to a protein ligand through the sulfhydryl group in a two-step process that allows the introduction of a disulfide bond between the ligand and the crosslinker. Incubation of the labelled ligand with oxidized live cells leads to the formation of crosslinks with aldehyde-containing glycans on the cell surface receptor. Subsequent reduction of the disulfide bond results in biotin transfer from the ligand to the cell surface receptor. Protein biotinylation that is mediated by ligand binding to its receptor is differentiated from background biotinylation events by comparison with a similarly labelled control protein using comparative proteomic mass spectrometry to quantify streptavidin-bound proteins. Using this method, we successfully identified the cell surface receptors of a peptide hormone, a monoclonal antibody, and a single-domain antibody-Fc fusion construct.

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Rabbit Anti-SEC14 like pr Rabbit Anti-Cell death in Anti C Reactive Protein A Bone Morphogenetic Protei Alpha-soluble NSF attachm MOUSE ANTI BORRELIA BURGD cell cycle progression 2 Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant Human Soluble Recombinant Human Soluble

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#28411555   2017/04/15 Save this To Up

Chemoproteomic profiling of targets of lipid-derived electrophiles by bioorthogonal aminooxy probe.

Redox imbalance in cells induces lipid peroxidation and generates a class of highly reactive metabolites known as lipid-derived electrophiles (LDEs) that can modify proteins and affects their functions. Identifying targets of LDEs is critical to understand how such modifications are functionally implicated in oxidative-stress associated diseases. Here we report a quantitative chemoproteomic method to globally profile protein targets and sites modified by LDEs. In this strategy, we designed and synthesized an alkyne-functionalized aminooxy probe to react with LDE-modified proteins for imaging and proteomic profiling. Using this probe, we successfully quantified >4000 proteins modified by 4-hydroxy-2-nonenal (HNE) of high confidence in mammalian cell lysate and combined with a tandem-orthogonal proteolysis activity-based protein profiling (TOP-ABPP) strategy, we identified ~400 residue sites targeted by HNE including reactive cysteines in peroxiredoxins, an important family of enzymes with anti-oxidant roles. Our method expands the toolbox to quantitatively profile protein targets of endogenous electrophiles and the enlarged inventory of LDE-modified proteins and sites will contribute to functional elucidation of cellular pathways affected by oxidative stress.

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5 (Octadecanoylamino)fluo 1 [4 (Dimethylamino)pheny 8 Octadecyloxypyrene 1,3, Ofloxacin CAS Number [824 HIV type O envelope antig CELLKINES PLATELET DERIVE PLATELET DERIVED GROWTH F CELLKINES PLATELET DERIVE PLATELET DERIVED GROWTH F Human Brain Derived Neuro Human Glial Derived Neuro Human Stromal Cell-Derive

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#28273378   2017/03/08 Save this To Up

The synthesis of [(14) C]4-acetylphenylalanine, effect on cell viability, and assessment of protein incorporation in male rat hepatocytes.

PEGylation is a proven approach to prolonging the duration of action and enhancing biophysical solubility and stability of peptides. 4-Acetylphenylalanine is a novel amino acid with a ketone side chain that is uniquely reactive in proteins. The ketone functionality can react with an aminooxy functionalized polyethyleneglycol polymer to form a stable oxime adduct of the protein. One concern with using unnatural amino acids, such as 4-acetylphenylalanine, is the possibility of it being cleaved from the peptide and becoming incorporated into endogenous proteins. To determine whether this occurs, an in vitro experiment to assess the cell viability and amino acid incorporation into endogenous proteins using primary male rat hepatocytes in the presence of [(14) C]4-acetylphenylalanine, 4 or [(14) C(U)]L-phenylalanine was conducted. [(14) C]4-acetylphenylalanine, 4 was prepared in 2 radiochemical steps from [1-(14) C]acetyl chloride in an overall 8% radiochemical yield and in 99.9% radiochemical purity. The results showed that there was no evidence of carbon-14 incorporation into hepatocyte endogenous proteins with [(14) C]pAcF and there was no difference between it and L-phenylalanine in cell viability assessments at any of the concentrations studied between 0.1 and 1000 μM.

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GLP 1 ELISA Kit, Rat Gluc GLP 2 ELISA Kit, Rat Prog Glucagon ELISA KIT, Rat G Leptin ELISA Kit, Rat Lep Rat Macrophage Inflammato Rabbit Anti-APIP Apaf1 In Rabbit Anti-APIP Apaf1 In Rabbit Anti-Cell death in Rabbit Anti-Cell death in Rabbit Anti-Cell death in Rabbit Anti-Cell death in Rabbit Anti-Cell death in

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