Enzymes and Inhibitors
Roche Diagnostics PROTEASE 1
Protease 1, Component: Proprietary ingredients, 45 to 55%, Sodium azide, CAS No.: 26628-22-8, 0.1%, Appearance: Clear, Colorless liquid, Odorless, Solubility: Miscible in water, pH: neutral, Stability: stable
Enzo Life Sciences Ubiquitin activating enzyme E1 (human), (recombinant) (His-tag) (50 µg)
Essential ubiquitinylation pathway enzyme. MW: 118 kDa. Purity: ≥90% (SDS-PAGE). Formulation: In 50mM TRIS-hydrochloric acid, containing 1.0mM dithiothreitol. Source: Produced in E. coli BL21 (λDE3) expression system and containing a C-terminal His6-tag. Full length human ubiquitin-activating enzyme E1. UniProt: P22314. Handling: Avoid freeze/thaw cycles. Long Term Storage: -80°C
Cayman Chemical N-Oleoyl-L-SerIn 50mg
An endogenous lipid that has been reported to stimulate bone formation and to inhibit bone resorption
Sigma Aldrich Fine Chemicals Biosciences Isovaleryl coenzyme A lith10MG
Isovaleryl coenzyme A an intermediate of the leucine catabolism. It is synthesized from -methylbutyric acid by the action of enzyme acyl CoA synthetase. The conversion of isovaleryl-CoA to methylcrotonyl-CoA is catalyzed by the enzyme isovaleryl-CoA dehydrogenase in leucine catabolism pathway. The enzyme isovaleryl-CoA oxidase also calalyzes this conversion in fatty acid -oxidation pathway.
Sigma Aldrich Fine Chemicals Biosciences Oleoyl 13C18 coenzyme A li10MG
Oleoyl 13C18 coenzyme A li10MG
Sigma Aldrich Fine Chemicals Biosciences 5 Hydroxyindole 3a45677a 11MG
5 Hydroxyindole 3a45677a 11MG
Sigma Aldrich Fine Chemicals Biosciences Crotonoyl coenzyme A trili25MG
Crotonoyl coenzyme A trili25MG
Sigma Aldrich Fine Chemicals Biosciences Malonyl 13C3 coenzyme A li10MG
Malonyl 13C3 coenzyme A li10MG
Immunology Consultants Hamster (CHO) Lysosomal Acid Lipase - Recombinant, 0.025mg
Recombinant CHO Lysosomal Acid Lipase (LAL; NCBI XP_035297776.1) is expressed in CHO cells with a 6xHIS tag and purified to >95% purity. LAL appears at ~55 kDa under reducing conditions and is quantified by A280. As a lipid‑metabolizing lysosomal enzyme, LAL can co‑purify with biologics and contribute to product degradation during purification or storage. This high‑quality recombinant antigen provides a reliable standard for ELISA development, antibody validation, and HCP profiling. Its CHO‑derived structure ensures biological relevance for impurity monitoring and process optimization. A valuable tool for teams studying lipid‑processing enzymes, assessing LAL‑related risks, or refining HCP detection workflows.
STEMCELL Technologies Dispase, ACF, Size: 10 mg
Dispase, Animal Component-Free (ACF) is a neutral, amino-endoprotease that cleaves the N-terminal peptide bond of non-polar amino acid residues and is obtained from cultures free of animal-derived materials. Dispase has mild proteolytic activity, which makes it especially useful for the isolation and passaging of primary cells. Its proteolytic activity also allows it to maintain membrane integrity. Dispase is commonly used with other proteases such as collagenase in cell isolation and tissue dissociation for neural tissue (Dietrich et al.), kidney (Presnell et al.), epithelial tissue (Smoot et al.), endothelial tissue (Müller et al.), lung (Barkauskas et al.), colon (Roig et al.), and stem cells (Thomson et al.; Salmon et al.).
Ubpbio SUC-LLVY-AMC, 5MG
Fluorescent Peptides/Protein Substrates – SUC-LLVY-AMC (UBPBio catalog# G1100, G1101) – Suc-LLVY-AMC is a fluorogenic substrate for the chymotrypsin – like activity of the 20S and 26S proteasomes. Working concentrations of this substrate is 50-200 µM. The released AMC can be detected by a fluorimeter or plate reader at excitation/emission wavelengths of 380 nm/460 nm, respectively. When used to determine proteasome activity in cell lysates, cell lysates that are pre-treated with a proteasome inhibitor such as MG132, PS341 or epoxomicin can be used to determine the fluorescence contributed by other cellular proteases that cleave this substrate. Readings from proteasome inhibitor-treated lysates should be subtracted.
Ubpbio HUMAN UBE1, 25UG
E1 Activating Enzymes – UbE1 (UBPBio catalog# B1100, B1101) – Purified from sf9 insect cells. UBE1 is an E1 enzyme within the E1, E2, E3 cascade which conjugates Ub to protein substrates. UBE1 activates Ub by catalyzing an ATP – dependent reaction; Ub is conjugated onto the catalytic Cys residue of UBE1 by formation of a thioester bond. The activated Ub is then passed onto a Ub-conjugating enzyme E2; Ub charged E2 binds a Ub ligase E3 that directly binds substrate proteins. Ub is transferred to the HECT domain E3s prior to being conjugated on substrate proteins. For RING domain E3s, Ub is transferred directly from an E2 to substrate proteins.