85 Results for: "1-Benzyl-azetidine-2-carboxylic acid amide"

This gene encodes a member of the nitrilase protein family with homology to bacterial and plant nitrilases, enzymes that cleave nitriles and organic amides to the corresponding carboxylic acids plus ammonia. Multiple transcript variants encoding different isoforms have been found for this gene.

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Mouse recombinant carboxypeptidase A2

Supplier: ProSci Inc.

Mouse carboxypeptidase A2(CPA2) is a secreted pancreatic procarboxy -peptidase which belongs to the peptidase M14 family. CPA2 consists of a signal peptide, a pro region and a mature chain. It can be activated after cleavage of the pro peptide. CPA2 cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan.

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Nitrocefin ≥95% (by UV method) dye, Calbiochem®, Sigma-Aldrich®

Supplier: Merck Millipore (Calbiochem‎)

A chromogenic β-lactamase substrate that undergoes distinctive color change from yellow (λmax = 390 nm at pH 7.0) to red (λmax = 486 nm at pH 7.0) as the amide bond in the β-lactam ring is hydrolyzed by β-lactamase

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Human recombinant Carboxypeptidase A2 (from Cells)

Supplier: ProSci Inc.

Carboxypeptidase A2 (CPA) is a secreted pancreatic procarboxy-peptidase that cleaves the C-terminal amide or ester bond of peptides that have a free C-terminal carboxyl group. The hydrolytic action of CPA2 was identified with a preference towards long substrates with aromatic amino acids in their C-terminal end, particularly tryptophan. CPA2 comprises a signal peptide, a pro region and a mature chain, and can be activated after cleavage of the pro peptide. Three different forms of human pancreatic procarboxypeptidase A have been isolated, and the A1 and A2 forms are always secreted as monomeric proteins with different biochemical properties. In contrast to procarboxypeptidase B which was always secreted by the pancreas as a monomer, procarboxypeptidase A occurs as a monomer and/or associated to one or two functionally different proteins, such as zymogen E, and is involved in zymogen inhibition.

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Mouse recombinant carboxylesterase 2E

Supplier: ProSci Inc.

Carboxylesterase 5 (CES5), also called cauxin or CES7, is a member of carboxylesterases family which plays an important role in the hydrolysis of ester and amide bonds. Carboxylesterase is a type of enzyme that capable of hydrolysing a variety of carboxylic acid esters and it's widely distributed in cells especially in mammalian liver. CES5 is with broad substrate specificity ranging from small molecule esters to longchain fatty acid esters and thioesters. It has been previously reported CES5 was in high concentrations in the urine (cauxin) of adult male cats, and within a protein complex of mammalian male epididymal fluids. Roles for CES5 may include regulating urinary levels of male cat pheromones, catalysing lipid transfer reactions within mammalian male reproductive fluids, and protecting neural tissue from drugs and xenobiotics.

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SMCC (N-Succinimidyl 4-(N-Maleimidomethyl)cyclohexanecarboxylate), No-Weigh™ Format, Pierce™

Supplier: Thermo Fisher Scientific

Thermo Scientific Pierce SMCC is a hetero-bifunctional crosslinker that contain N-hydroxysuccinimide (NHS) ester and maleimide groups that allow covalent conjugation of amine- and sulfhydryl-containing molecules. NHS esters react with primary amines at pH 7–9 to form amide bonds, while maleimides react with sulfhydryl groups at pH 6.5–7.5 to form stable thioether bonds. In aqueous solutions, NHS ester hydrolytic degradation is a competing reaction whose rate increases with pH. The maleimide group is more stable than the NHS-ester group, but will slowly hydrolyze and lose its reaction specificity for sulfhydryls at pH values > 7.5. For these reasons, conjugations with these crosslinkers are usually performed at pH 7.2–7.5, with the NHS ester (amine-targeted) reacted before or simultaneous with the maleimide (sulfhydryl-targeted) reaction.

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SMCC (N-Succinimidyl 4-(N-Maleimidomethyl)cyclohexanecarboxylate) ≥85%

Supplier: AAT BIOQUEST

SMCC is a non-cleavable and membrane permeable crosslinker with a spacer arm of 8.3 Å. It contains an amine-reactive succinimidyl ester (SE) and a sulfhydryl-reactive maleimide group. NHS esters react with primary amines at pH 7 to 9 to form stable amide bonds. Maleimides react with sulfhydryl groups at pH 6.5 to 7.5 to form stable thioether bonds. The SE group of SMCC is reacted with lysine residues on the carrier protein, converting them to reactive maleimides. SMCC is a reagent that is widely used for generating stable maleimide-activated carrier proteins that can spontaneously react with sulfhydryls. Alternatively these relatively stable maleimide-activated intermediates may be lyophilized and stored for later conjugation to a hapten.