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Merck
CN

516483

Pepstatin A, Penetratin

A Pepstatin A that is ~75% less potent against Cathespins D/E than PepA in cell-free assays.

Synonym(s):

Pepstatin A, Penetratin, PepA-RQIKIWFQNRRMKWKK-OH, PepA-Antp43₋58

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About This Item

Empirical Formula (Hill Notation):
C138H229N39O28S
Molecular Weight:
2914.60
NACRES:
NA.77
UNSPSC Code:
12352202

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Product Name

Pepstatin A, Penetratin, A Pepstatin A that is ~75% less potent against Cathespins D/E than PepA in cell-free assays.

assay

≥97% (HPLC)

form

lyophilized solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze
desiccated (hygroscopic)
protect from light

color

white

solubility

water: 1 mg/mL

shipped in

wet ice

storage temp.

−20°C

Quality Level

100

Other Notes

Zaidi, N., et al. 2007. Biochem. Biophys. Res. Commun.364, 243.
PepA-Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys-CO₂H

Packaging

Packaged under inert gas

Physical form

Supplied as a trifluoroacetate salt.

Disclaimer

Toxicity: Standard Handling (A)

General description

A Pepstatin A (PepA; Cat. No. 516481) penetratin (pAntp43-58) conjugate (PepA-P) that is ~75% less potent against Cathespins D/E (IC50 = 920 nM) than PepA in cell-free assays, presumably due to its decreased solubility. However, with its enhanced permeability, PepA-P is much more active than PepA in inhibiting cellular aspartic protease activity in MCF7 (94.1% vs. 54.6% inhibition wtih 10 µM respective compound), Boleths, and Dendritic cultures. PepA-P, but not PepA, effectively interferes with antigen processing by primary APCs and the subsequent activation of antigen-specific memory T cells.

Preparation Note

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

Legal Information

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

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

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Adrienn Skopál et al.
The Journal of biological chemistry, 298(5), 101888-101888 (2022-04-04)
Adenosine A2A receptor (A2AR)-dependent signaling in macrophages plays a key role in the regulation of inflammation. However, the processes regulating A2AR targeting to the cell surface and degradation in macrophages are incompletely understood. For example, the C-terminal domain of the

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