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SML0430

Sigma-Aldrich

PR-619

≥95% (HPLC)

Synonym(s):

2,6-Diamino-3,5-dithiocyanopyridine, Thiocyanic acid C,C′-(2,6-diamino-3,5-pyridinediyl) ester; 2,6-Diaminopyridine-3,5-bis(thiocyanate)

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About This Item

Empirical Formula (Hill Notation):
C7H5N5S2
CAS Number:
2645-32-1
Molecular Weight:
223.28
MDL number:
MFCD00830384
UNSPSC Code:
12352200
PubChem Substance ID:
329825425
NACRES:
NA.77
Pricing and availability is not currently available.

Quality Level

100

Assay

≥95% (HPLC)

form

powder

color

white to beige

solubility

DMSO: 5 mg/mL (clear solution)

storage temp.

−20°C

SMILES string

Nc1nc(N)c(SC#N)cc1SC#N

InChI

1S/C7H5N5S2/c8-2-13-4-1-5(14-3-9)7(11)12-6(4)10/h1H,(H4,10,11,12)

InChI key

ZXOBLNBVNROVLC-UHFFFAOYSA-N

Application

PR-619 has been used:
  • as a component of lysis buffer and also as a deubiquitinase inhibitor to treat proteins derived from SILAC-labeled Jurkat cells[1]
  • as a pan-deubiquitinase inhibitor to study its effect on adenoassociated virus (AAV) transduction[2]
  • in radioimmunoprecipitation assay buffer (RIPA) buffer used for ubiquitination assays[3]

Biochem/physiol Actions

PR-619 is a cell permeable broad spectrum deubiquitylating enzymes (DBUs) inhibitor. PR-619 induces the accumulation of polyubiquitylated proteins in cells without directly affecting proteasome activity.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

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Certificates of Analysis (COA)

Lot/Batch Number
0000190433
0000190431
096M4762V
045M4727V
072M4748V

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Anne Garreau et al.
Journal of immunology (Baltimore, Md. : 1950), 199(8), 2758-2766 (2017-09-08)
Themis is a new component of the TCR signaling machinery that plays a critical role during T cell development. The positive selection of immature CD4
Large-scale identification of ubiquitination sites by mass spectrometry
Udeshi ND, et al.
Nature Protocols, 8(10), 1950-1950 (2013)
Yang Wang et al.
Animal reproduction science, 187, 64-73 (2017-10-17)
This study was undertaken to investigate the dynamics of protein ubiquitination in pig gametes and their micro-environments, as well as to explore the action of deubiquitinases (DUBs) in sperm-oocyte binding. Protein ubiquitination states were evaluated by in the ejaculated sperm
Hirotaka Takahashi et al.
Biomedicines, 8(6) (2020-06-10)
Protein ubiquitinations play pivotal roles in many cellular processes, including homeostasis, responses to various stimulations, and progression of diseases. Deubiquitinating enzymes (DUBs) remove ubiquitin molecules from ubiquitinated proteins and cleave the polyubiquitin chain, thus negatively regulating numerous ubiquitin-dependent processes. Dysfunctions
Rudolf Lucas et al.
The Journal of biological chemistry, 291(45), 23440-23451 (2016-09-21)
Regulation of the epithelial sodium channel (ENaC), which regulates fluid homeostasis and blood pressure, is complex and remains incompletely understood. The TIP peptide, a mimic of the lectin-like domain of TNF, activates ENaC by binding to glycosylated residues in the
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