Fluorogenic Chymotrypsin Substrate II
<strong>Fluorogenic Chymotrypsin Substrate II</strong>_x000D_ <strong>Catalog number:</strong> B2013080_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 5 mg_x000D_ <strong>Molecular Weight or Concentration:</strong> 661.7 g/mol_x000D_ <strong>Supplied as:</strong> Lyophilized Powder_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20°C_x000D_ <strong>Keywords:</strong> Chymotrypsin Substrate II, Fluorogenic_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Al-Abdullah IH, Bagramyan K, Bilbao S, Qi M, Kalkum M. Fluorogenic Peptide Substrate for Quantification of Bacterial Enzyme Activities Sci Rep. 2017 Mar 13;7:44321._x000D_ 2: Nedungadi D, Binoy A, Pandurangan N, Pal S, Nair BG, Mishra N. 6-Shogaol induces caspase-independent paraptosis in cancer cells via proteasomal inhibition Exp Cell Res. 2018 Mar 15;364(2):243-251._x000D_ 3: Raymond WW, Ruggles SW, Craik CS, Caughey GH. Albumin is a substrate of human chymase. Prediction by combinatorial peptide screening and development of a selective inhibitor based on the albumin cleavage site J Biol Chem. 2003 Sep 5;278(36):34517-24._x000D_ 4: Nehybová T, Šmarda J, Daniel L, Stiborek M, Kanický V, Spasojevič I, Preisler J, Damborský J, Beneš P. Wedelolactone Acts as Proteasome Inhibitor in Breast Cancer Cells Int J Mol Sci. 2017 Mar 29;18(4):729._x000D_ 5: Nozawa M, Tanizawa K, Kanaoka Y. New chromogenic and fluorogenic substrates for the determination of butyrylcholinesterase and arylesterase activities J Pharmacobiodyn. 1980 Jul;3(7):321-7._x000D_ 6: Harding CV, France J, Song R, Farah JM, Chatterjee S, Iqbal M, Siman R. Novel dipeptide aldehydes are proteasome inhibitors and block the MHC-I antigen-processing pathway J Immunol. 1995 Aug 15;155(4):1767-75._x000D_ 7: Le QT, Ohashi A, Hirose S, Katunuma N. Reverse zymography using fluorogenic substrates for protease inhibitor detection Electrophoresis. 2005 Mar;26(6):1038-45._x000D_ 8: Semashko TA, Lysogorskaia EN, Oksenoĭt ES, Bacheva AV, Filippova IIu. [Chemoenzymatic synthesis of new fluorogenous substrates for cysteine proteases of the papain family] Bioorg Khim. 2008 May-Jun;34(3):376-81._x000D_ 9: Gohlke S, Kloss A, Tsokos M, Textoris-Taube K, Keller C, Kloetzel PM, Dahlmann B. Adult human liver contains intermediate-type proteasomes with different enzymatic properties Ann Hepatol. 2014 Jul-Aug;13(4):429-38._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/3304342">10: Moroder L, Bovermann G, Mourier G, Göhring W, Gemeiner M, Wünsch E. Studies on immunoassays of peptide factors. II. Fluorescence enzyme immunoassay for human little-gastrin Biol Chem Hoppe Seyler. 1987 Jul;368(7):831-8. </a>_x000D_ _x000D_ <strong>Products Related to Fluorogenic Chymotrypsin Substrate II can be found at</strong> <a href="https://moleculardepot.com/product-category/Substrates/"> Substrates</a>
Product Specifications
Short Description
Catalog Number: B2013080 (5 mg)
Weight
0.8
Length
2
Width
0.9
Height
0.9
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