CLIK-148

    WARNING: This product is for research use only, not for human or veterinary use.

Hodoodo CAT#: H130007

CAS#: 215098-90-1

Description: CLIK-148 is a Cathepsin L specific inhibitor. CLIK-148 inhibitor treatment resulted in decreased amounts of CCK secreted from the regulated secretory pathway of AtT-20 cells. CLIK-148 also reduced cellular levels of CCK9 (Arg-CCK8), consistent with CCK9 as an intermediate product of cathepsin L, shown by the decreased ratio of CCK9/CCK8.

Chemical Structure

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CLIK-148
CAS# 215098-90-1
Instruction

Theoretical Analysis

Hodoodo Cat#: H130007
Name: CLIK-148
CAS#: 215098-90-1
Chemical Formula: C22H26N4O4
Exact Mass: 410.20
Molecular Weight: 410.470
Elemental Analysis: C, 64.37; H, 6.38; N, 13.65; O, 15.59

Price and Availability

This product is not in stock, which may be available by custom synthesis. For cost-effective reason, minimum order is 1g (price is usually high, lead time is 2~3 months, depending on the technical challenge). Quote less than 1g will not be provided. To request quote, please email to sales @hodoodo.com or click below button.
Note: Price will be listed if it is available in the future.

Request quote for custom synthesis

Synonym: CLIK-148; CLIK148; CLIK 148

IUPAC/Chemical Name: (2S,3S)-2-N-[(2S)-1-(Dimethylamino)-1-oxo-3-phenylpropan-2-yl]-3-N-(2-pyridin-2-ylethyl)oxirane-2,3-dicarboxamide

InChi Key: SXMRSAGDCJGMTG-FHWLQOOXSA-N

InChi Code: InChI=1S/C22H26N4O4/c1-26(2)22(29)17(14-15-8-4-3-5-9-15)25-21(28)19-18(30-19)20(27)24-13-11-16-10-6-7-12-23-16/h3-10,12,17-19H,11,13-14H2,1-2H3,(H,24,27)(H,25,28)/t17-,18-,19-/m0/s1

SMILES Code: O=C([C@H]1O[C@@H]1C(NCCC2=NC=CC=C2)=O)N[C@@H](CC3=CC=CC=C3)C(N(C)C)=O

Appearance: To be determined

Purity: >98% (or refer to the Certificate of Analysis)

Shipping Condition: Shipped under ambient temperature as non-hazardous chemical. This product is stable enough for a few weeks during ordinary shipping and time spent in Customs.

Storage Condition: Dry, dark and at 0 - 4 C for short term (days to weeks) or -20 C for long term (months to years).

Solubility: To be determined

Shelf Life: >2 years if stored properly

Drug Formulation: To be determined

Stock Solution Storage: 0 - 4 C for short term (days to weeks), or -20 C for long term (months).

HS Tariff Code: 2934.99.9001

More Info:

Biological target:
In vitro activity:
In vivo activity:

Preparing Stock Solutions

The following data is based on the product molecular weight 410.47 Batch specific molecular weights may vary from batch to batch due to the degree of hydration, which will affect the solvent volumes required to prepare stock solutions.

Recalculate based on batch purity %
Concentration / Solvent Volume / Mass 1 mg 5 mg 10 mg
1 mM 1.15 mL 5.76 mL 11.51 mL
5 mM 0.23 mL 1.15 mL 2.3 mL
10 mM 0.12 mL 0.58 mL 1.15 mL
50 mM 0.02 mL 0.12 mL 0.23 mL
Formulation protocol:
In vitro protocol:
In vivo protocol:

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1: Jakoš T, Pišlar A, Pečar Fonović U, Švajger U, Kos J. Cysteine cathepsins L and X differentially modulate interactions between myeloid-derived suppressor cells and tumor cells. Cancer Immunol Immunother. 2020 Sep;69(9):1869-1880. doi: 10.1007/s00262-020-02592-x. Epub 2020 May 5. PMID: 32372139.


2: Huisman M, Kodanko JP, Arora K, Herroon M, Alnaed M, Endicott J, Podgorski I, Kodanko JJ. Affinity-Enhanced Luminescent Re(I)- and Ru(II)-Based Inhibitors of the Cysteine Protease Cathepsin L. Inorg Chem. 2018 Jul 2;57(13):7881-7891. doi: 10.1021/acs.inorgchem.8b00978. Epub 2018 Jun 8. PMID: 29882662; PMCID: PMC6034508.


3: Xu M, Yang L, Rong JG, Ni Y, Gu WW, Luo Y, Ishidoh K, Katunuma N, Li ZS, Zhang HL. Inhibition of cysteine cathepsin B and L activation in astrocytes contributes to neuroprotection against cerebral ischemia via blocking the tBid- mitochondrial apoptotic signaling pathway. Glia. 2014 Jun;62(6):855-80. doi: 10.1002/glia.22645. Epub 2014 Feb 24. PMID: 24616078.


4: Gu WW, Ao GZ, Zhu YM, Sun SC, Zhou Q, Fan JH, Nobuhiko K, Ishidoh K, Zhang HL, Gao XM. Autophagy and cathepsin L are involved in the antinociceptive effect of DMBC in a mouse acetic acid-writhing model. Acta Pharmacol Sin. 2013 Aug;34(8):1007-12. doi: 10.1038/aps.2013.30. PMID: 23912553; PMCID: PMC4003021.


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6: Katunuma N. Structure-based development of specific inhibitors for individual cathepsins and their medical applications. Proc Jpn Acad Ser B Phys Biol Sci. 2011;87(2):29-39. doi: 10.2183/pjab.87.29. PMID: 21321479; PMCID: PMC3043741.


7: Pucer A, Castino R, Mirković B, Falnoga I, Slejkovec Z, Isidoro C, Lah TT. Differential role of cathepsins B and L in autophagy-associated cell death induced by arsenic trioxide in U87 human glioblastoma cells. Biol Chem. 2010 May;391(5):519-31. doi: 10.1515/BC.2010.050. PMID: 20302512.


8: Katunuma N. [Structure-based drug development and medical/biological application of cathepsin specific inhibitors]. Seikagaku. 2009 Nov;81(11):952-61. Japanese. PMID: 19999577.


9: Yoshii H, Kamiyama H, Minematsu K, Goto K, Mizota T, Oishi K, Katunuma N, Yamamoto N, Kubo Y. Cathepsin L is required for ecotropic murine leukemia virus infection in NIH3T3 cells. Virology. 2009 Nov 25;394(2):227-34. doi: 10.1016/j.virol.2009.08.045. Epub 2009 Sep 24. PMID: 19781728; PMCID: PMC7111982.


10: Beinfeld MC, Funkelstein L, Foulon T, Cadel S, Kitagawa K, Toneff T, Reinheckel T, Peters C, Hook V. Cathepsin L plays a major role in cholecystokinin production in mouse brain cortex and in pituitary AtT-20 cells: protease gene knockout and inhibitor studies. Peptides. 2009 Oct;30(10):1882-91. doi: 10.1016/j.peptides.2009.06.030. Epub 2009 Jul 7. PMID: 19589362; PMCID: PMC2755599.


11: Funkelstein L, Toneff T, Mosier C, Hwang SR, Beuschlein F, Lichtenauer UD, Reinheckel T, Peters C, Hook V. Major role of cathepsin L for producing the peptide hormones ACTH, beta-endorphin, and alpha-MSH, illustrated by protease gene knockout and expression. J Biol Chem. 2008 Dec 19;283(51):35652-9. doi: 10.1074/jbc.M709010200. Epub 2008 Oct 10. PMID: 18849346; PMCID: PMC2602888.


12: Beavers MP, Myers MC, Shah PP, Purvis JE, Diamond SL, Cooperman BS, Huryn DM, Smith AB 3rd. Molecular docking of cathepsin L inhibitors in the binding site of papain. J Chem Inf Model. 2008 Jul;48(7):1464-72. doi: 10.1021/ci800085c. Epub 2008 Jul 4. Erratum in: J Chem Inf Model. 2010 Dec 27;50(12):2274. PMID: 18598021; PMCID: PMC2923042.


13: Shah PP, Myers MC, Beavers MP, Purvis JE, Jing H, Grieser HJ, Sharlow ER, Napper AD, Huryn DM, Cooperman BS, Smith AB 3rd, Diamond SL. Kinetic characterization and molecular docking of a novel, potent, and selective slow- binding inhibitor of human cathepsin L. Mol Pharmacol. 2008 Jul;74(1):34-41. doi: 10.1124/mol.108.046219. Epub 2008 Apr 10. PMID: 18403718; PMCID: PMC2575030.


14: Yang M, Zhang Y, Pan J, Sun J, Liu J, Libby P, Sukhova GK, Doria A, Katunuma N, Peroni OD, Guerre-Millo M, Kahn BB, Clement K, Shi GP. Cathepsin L activity controls adipogenesis and glucose tolerance. Nat Cell Biol. 2007 Aug;9(8):970-7. doi: 10.1038/ncb1623. Epub 2007 Jul 22. PMID: 17643114.


15: Onishi K, Li Y, Ishii K, Hisaeda H, Tang L, Duan X, Dainichi T, Maekawa Y, Katunuma N, Himeno K. Cathepsin L is crucial for a Th1-type immune response during Leishmania major infection. Microbes Infect. 2004 Apr;6(5):468-74. doi: 10.1016/j.micinf.2004.01.008. PMID: 15109961.


16: Stern I, Schaschke N, Moroder L, Turk D. Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft. Biochem J. 2004 Jul 15;381(Pt 2):511-7. doi: 10.1042/BJ20040237. PMID: 15084146; PMCID: PMC1133859.


17: Katunuma N, Matsunaga Y, Himeno K, Hayashi Y. Insights into the roles of cathepsins in antigen processing and presentation revealed by specific inhibitors. Biol Chem. 2003 Jun;384(6):883-90. doi: 10.1515/BC.2003.099. PMID: 12887055.


18: Katunuma N, Tsuge H, Nukatsuka M, Fukushima M. Structure-based development of cathepsin L inhibitors and therapeutic applications for prevention of cancer metastasis and cancer-induced osteoporosis. Adv Enzyme Regul. 2002;42:159-72. doi: 10.1016/s0065-2571(01)00060-7. PMID: 12123713.


19: Sever N, Filipic M, Brzin J, Lah TT. Effect of cysteine proteinase inhibitors on murine B16 melanoma cell invasion in vitro. Biol Chem. 2002 May;383(5):839-42. doi: 10.1515/BC.2002.088. PMID: 12108549.


20: Katunuma N, Tsuge H, Nukatsuka M, Asao T, Fukushima M. Structure-based design of specific cathepsin inhibitors and their application to protection of bone metastases of cancer cells. Arch Biochem Biophys. 2002 Jan 15;397(2):305-11. doi: 10.1006/abbi.2001.2709. PMID: 11795887.