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Key Documents

219372

Sigma-Aldrich

Cathepsin G Inhibitor I

≥98% (HPLC), solid, cathepsin G inhibitor, Calbiochem®

Sinónimos:

Cathepsin G Inhibitor I

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About This Item

Fórmula empírica (notación de Hill):
C36H33N2O6P
Número de CAS:
429676-93-7
Peso molecular:
620.63
UNSPSC Code:
12352200
NACRES:
NA.77

product name

Cathepsin G Inhibitor I, The Cathepsin G Inhibitor I, also referenced under CAS 429676-93-7, controls the biological activity of Cathepsin G. This small molecule/inhibitor is primarily used for Protease Inhibitors applications.

Quality Level

100

assay

≥98% (HPLC)

form

solid

potency

53 nM IC50

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
protect from light

color

white

solubility

DMSO: 5 mg/mL
methanol: soluble

shipped in

ambient

storage temp.

−20°C

InChI

1S/C36H33N2O6P/c1-37(28-18-20-38(21-19-28)35(40)25-11-3-2-4-12-25)36(41)32-23-27-14-6-5-13-26(27)22-31(32)33(39)34(45(42,43)44)30-17-9-15-24-10-7-8-16-29(24)30/h2-17,22-23,28,34H,18-21H2,1H3,(H2,42,43,44)

InChI key

GNOZQRKYZJSIPZ-UHFFFAOYSA-N

General description

A potent, selective, reversible, and competitive non-peptide inhibitor of cathepsin G (IC50 = 53 nM and Ki = 63 nM). Weakly inhibits chymotrypsin (Ki = 1.5 µM) and does not have any significant inhibitory effect on thrombin, factor Xa, factor IXa, plasmin, trypsin, tryptase, proteinase 3, and human leukocyte elastase (IC50 >100 µM).
A potent, selective, reversible, competitive, non-peptide inhibitor of cathepsin G [IC50 = 53 nM and Ki = 63 nM]. Weakly inhibits chymotrypsin (Ki = 1.5 µM) and poorly inhibits thrombin, factor Xa, factor IXa, plasmin, trypsin, tryptase, proteinase 3, and human leukocyte elastase (IC50 >100 µM).

Biochem/physiol Actions

Cell permeable: no
Primary Target
cathepsin G
Product does not compete with ATP.
Reversible: yes
Target Ki: 63 nM for cathepsin G

Packaging

Packaged under inert gas

Warning

Toxicity: Standard Handling (A)

Reconstitution

Following reconstitution aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.

Other Notes

Greco, M.N., et al. 2002. J. Am. Chem. Soc.124, 3810.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Stefan J Schunk et al.
Circulation, 144(11), 893-908 (2021-07-02)
Cardiovascular diseases and chronic kidney disease (CKD) are highly prevalent, aggravate each other, and account for substantial mortality. Both conditions are characterized by activation of the innate immune system. The alarmin interleukin-1α (IL-1α) is expressed in a variety of cell
Fabian Gärtner et al.
ACS omega, 5(43), 28233-28238 (2020-11-10)
During an immune response, cathepsin G (CatG) takes on the role of adaptive and innate immunity and the outcome depends on the localization of CatG. Soluble, cell surface-bound, or intracellular CatG is also responsible for pathophysiology conditions. We applied the
Mira Tohmé et al.
Methods in molecular biology (Clifton, N.J.), 960, 509-515 (2013-01-19)
Proteases generate peptides that bind to MHC class II molecules to interact with a wide diversity of CD4(+) T cells. They are expressed in dedicated organelles: endosomes and lysosomes of professional antigen presenting cells (pAPCs) such as B cells, macrophages
Yueling Ouyang et al.
Veterinary research, 55(1), 22-22 (2024-02-20)
Clinically, Landrace pigs are more susceptible to porcine circovirus-associated diseases (PCVADs) than Piétrain pigs. We previously found that porcine circovirus type 2 (PCV2) can infect T-lymphoblasts. The present study examined the replication kinetics of six PCV2 strains in the lymphoblasts
Hui Yang et al.
EMBO reports, 24(10), e57032-e57032 (2023-08-31)
Bromodomain-containing protein 4 (BRD4) is overexpressed and functionally implicated in various myeloid malignancies. However, the role of BRD4 in normal hematopoiesis remains largely unknown. Here, utilizing an inducible Brd4 knockout mouse model, we find that deletion of Brd4 (Brd4Δ/Δ )
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