AdipoGen Life Sciences

Z-Leu-Arg-Gly-Gly-AMC

CHF 55.00
In stock
AG-CP3-0023-M0011 mgCHF 55.00
AG-CP3-0023-M0055 mgCHF 130.00
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Product Details
Synonyms Z-LRGG-AMC . TFA; UCH Substrate
Product Type Chemical
Properties
Formula

C34H44N8O8 . C2HF3O2

MW 692.8 . 114.0
Sequence

Z-Leu-Arg-Gly-Gly-7-amido-4-methylcoumarin

CAS 167698-68-2 (free base)
Purity Chemicals ≥95% (HPLC)
Appearance Solid lyophilized powder.
Solubility Soluble in 10% acetic acid.
Other Product Data

Use: Add from DMSO stock directly to in vitro or in vivo assays at desired concentration. Typical concentrations range from 10-100µM.

InChi Key OHFBLWHOBJRDAB-CCQIZPNASA-N
Smiles CC(C)C[C@H](NC(=O)OCC1=CC=CC=C1)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NCC(=O)NC1=CC2=C(C=C1)C(C)=CC(=O)O2
Shipping and Handling
Shipping AMBIENT
Short Term Storage +4°C
Long Term Storage -20°C
Handling Advice Avoid freeze/thaw cycles.
Protect from light.
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
Documents
MSDS Download PDF
Product Specification Sheet
Datasheet Download PDF
Description
  • Fluorogenic tetrapeptide substrate for ubiquitin C-terminal hydrolases (UCHs, e.g. UCHL3) and isopeptidase T.
  • LRGG is the preferred substrate sequence of the human deSUMOylating enzymes SENP6 and SENP7 [3].
  • Excitation: 380nm. Emission: 460nm.
Product References
  1. The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme: H.A. Lindner, et al.; J. Virol. 79, 15199 (2005)
  2. Biochemical characterization of USP7 reveals post-translational modification sites and structural requirements for substrate processing and subcellular localization: A. Fernandez-Montalvan, et al.; FEBS J. 274, 4256 (2007)
  3. Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family: M. Drag, et al.; Biochem. J. 409, 461 (2008)
  4. Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features: J. Lei, et al.; Antivir. Res. 109, 72 (2014)
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