substrate

4-Methylumbelliferyl-β-D-Glucopyranoside (4-MU-GLU) is used in the GCase activity assay based on the catalytic hydrolysis of 4-methylumbelliferyl β-D-glucopyranoside that releases the highly fluorescent 4-methylumbelliferyl (4-MU).

TMPD dihydrochloride is an active substrate of enzymatically convert redox and an electron donor for the reduction of heme peroxidases.

Arazine (N-Acetyl-S-farnesyl-L-cysteine) is a cell-permeable modulator of G protein and GPCR signaling, and it can act as a substrate for isoprenylcysteine methyltransferase by competing with prenylated G protein or its receptor sites.

Galanthamine N-Oxide, an alkaloid extracted from Zephyranthes concolor bulbs, effectively inhibits acetylcholinesterase (AChE) from electric eel with an EC50 of 26.2 μM. It acts as a significant inhibitor of substrate accommodation within the active sites of Torpedo californica AChE (TcAChE), human AChE (hAChE), and human BChE (hBChE) enzymes.

Nadolol is a non-selective beta-adrenergic antagonist with antihypertensive and antiarrhythmic activities. Nadolol competitively blocks beta-1 adrenergic receptors located in the heart and vascular smooth muscle, inhibiting the activities of the catechola

4-Nitrophenyl α-D-galactopyranoside (PNP-alpha-D-Gal) is an artificial substrate of 4-nitrophenyl (pNP) glycopyranoside used for detecting α-galactosidase activity. The amount of released pNP increases significantly when PNP-alpha-D-Gal is used as a substrate.

H-D-Phe-Pip-Arg-pNA dihydrochloride (S-2238 dihydrochloride), a chromogenic substrate, mimics the N-terminal fragment of the A alpha chain of fibrinogen, the native substrate of thrombin. Specifically designed for thrombin detection, it is employed for quantifying antithrombin-heparin cofactor (AT-III) and is characterized by its sensitivity, accuracy, and ease of implementation.

trans-4-Hydroxycyclohexanecarboxylic Acid is an organic intermediate.

Convallatoxin is a natural product

MBP MAPK Substrate acetate can be used as an exogenous substrate for MAPK.

Protein Kinase C Peptide Substrate acetate targets specific cell spacers ina manner that is dependent on second messengers and specific adaptor proteins in response to extracellular signals that activate g protein-coupled receptors, tyrosine Kinase recept

Sakamototide substrate peptide acetate is a peptide substrate of AMPK kinase family and can be used for the determination of kinase activity.

Calcineurin substrate acetate is from the regulatory RII subunit of cAMP-dependent protein kinase.

PKG Substrate acetate is a selective substrate for cGMP-dependent protein kinase (PKG).PKG Substrate is a selective substrate for protein kinase G (PKG) with a strong preference for PKG Iα (Km = 59 μM) over PKG II (Km = 305 μM).

HSV-TK substrate is an antitumor agent that induces multi-log cytotoxicity in both HSV-TK-expressing and bystander cells.

NQO1 substrate is a highly potent NQO1 substrate with potential antitumor activity for leukemia research.

The renin fluorogenic substrate consists of the normal peptide substrate for renin which has been linked to the fluorophore EDANS at one end and to a non-fluorescent quenching molecule (Dabcyl) at the other. After cleavage by renin, the product (peptide-EDANS) is brightly fluorescent and can be easily analyzed using an excitation wavelength of 340 nm and emission wavelengths of 485-510 nm.

Enteropeptidase fluorogenic substrate is a substrate for enteropeptidase that contains a 7-amino-4-trifluoromethylcoumarin (AFC) moiety. Enteropeptidase is a serine protease expressed in the proximal small intestine of higher animals that converts inactive trypsinogen to active trypsin by endoproteolytic cleavage. Enteropeptidase recognizes the highly specific amino acid sequence DDDDK on the fluorogenic substrate and cleaves after the lysine residue, releasing the AFC moiety. Enteropeptidase activity is quantified by fluorescent detection of AFC, which displays excitation/emission spectra of 380/500 nm.

Enteropeptidase fluorogenic substrate is a substrate for enteropeptidase that contains a 7-amino-4-trifluoromethylcoumarin (AFC) moiety. Enteropeptidase is a serine protease expressed in the proximal small intestine of higher animals that converts inactive trypsinogen to active trypsin by endoproteolytic cleavage.1,2Enteropeptidase recognizes the highly specific amino acid sequence DDDDK on the fluorogenic substrate and cleaves after the lysine residue, releasing the AFC moiety. Enteropeptidase activity is quantified by fluorescent detection of AFC, which displays excitation/emission spectra of 380/500 nm.3

Cyclin-dependent kinase 5 (Cdk5) is a serine/threonine kinase that is predominantly active in neuronal tissues. With p25 or p35, Cdk5 phosphorylates a range of proteins, including histone H1 and tau. Cdk5 substrate is a synthetic peptide (PKTPKKAKKL) corresponding to a sequence of histone H1. It is phosphorylated by Cdk5 with a Km value of 5 μM.

Cyclin-dependent kinase 5 (Cdk5) is a serine/threonine kinase that is predominantly active in neuronal tissues. With p25 or p35, Cdk5 phosphorylates a range of proteins, including histone H1 and tau. Cdk5 Substrate acetate is a synthetic peptide (PKTPKKAKKL) corresponding to a sequence of histone H1. It is phosphorylated by Cdk5 with a Km value of 5 µM.

Mca-GKPILFFRL-Dpa-r-amide, FRET substrate for cathepsin D and E. Also cleaved by napsin A.

Cathepsin D and E FRET Substrate acetate is a fluorogenic substrate for cathepsins D and E but not for B, H, or L. Cathepsin D and E FRET Substrate acetate can be used in mechanistic studies on cathepsins D and E studies.

Cathepsin D and E FRET Substrate acetate is a fluorogenic substrate selectively cleaved by cathepsins D and E at the Phe-Phe amide bond, demonstrating no activity towards cathepsins B, H, or L. This specificity renders it essential for routine assays and mechanistic studies focusing on cathepsins E and D[1].