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AB144641

PR 619, DUB inhibitor

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(11 Publications)

MW 223.3 Da, Purity >99%. Cell-permeable, non-selective and reversible DUB inhibitor (IC50 values are 5 to 20 μM). Induces polyubiquitinated protein accumulation in cells without directly affecting proteasome activity. Activates autophagy.

Key facts

CAS number

2645-32-1

Purity

>99%

Form

Solid

form

Molecular weight

223.3 Da

Molecular formula

C<sub>7</sub>H<sub>5</sub>N<sub>5</sub>S<sub>2</sub>

PubChem

2817763

Nature

Synthetic

Solubility

Soluble in DMSO to 100 mM

Biochemical name

3,5-Dithiocyanatopyridine-2,6-diamine

Biological description

Cell-permeable, non-selective and reversible DUB inhibitor (IC50 values are 5 to 20 μM). Induces polyubiquitinated protein accumulation in cells without directly affecting proteasome activity. Activates autophagy.

Canonical smiles

C1=C(C(=NC(=C1SC#N)N)N)SC#N

InChi

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

InChiKey

ZXOBLNBVNROVLC-UHFFFAOYSA-N

IUPAC Name

(2,6-diamino-5-thiocyanatopyridin-3-yl) thiocyanate

Properties and storage information

Shipped at conditions
Ambient - Can Ship with Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Store under desiccating conditions|The product can be stored for up to 12 months
Handling instructions

Need more advice on solubility, usage and handling? Please visit our our product support page for more details.

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Wherever possible, you should prepare and use solutions on the same day. However, if you need to make up stock solutions in advance, we recommend that you store the solution as aliquots in tightly sealed vials at -20°C. Generally, these will be useable for up to one month. Before use, and prior to opening the vial we recommend that you allow your product to equilibrate to room temperature for at least 1 hour.

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Refer to SDS for further information.

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Girdin also known as GIV or Girders of actin filaments plays a significant role in cell signaling. It is a multifunctional adaptor protein with a mass of approximately 220 kDa. GIV is expressed in various tissues including the brain heart and immune cells. It acts as an important player in the reorganization of the actin cytoskeleton which is critical for cellular processes like migration and adhesion.
Biological function summary

GIV is important for modulating signal transduction pathways. It interacts with G-protein coupled receptors (GPCRs) and growth factor receptors facilitating the activation of G-protein signaling. GIV does not typically function alone; it integrates into larger signaling complexes interfacing with other proteins to propagate signals downstream. Through these interactions it influences processes like cell proliferation and survival.

Pathways

GIV significantly impacts the PI3K-Akt and MAPK pathways. It acts as an upstream regulator controlling the activation of signaling cascades that determine cell fate decisions. GIV works closely with proteins such as Akt a central protein in the PI3K pathway and Grb2 linking receptor tyrosine kinases to downstream signaling mechanisms. These interactions highlight GIV’s importance in mediating cellular responses to external stimuli.

GIV’s dysregulation links to cancer and metabolic disorders. In cancer GIV overexpression correlates with enhanced tumor progression and poor patient prognosis. GIV interacts with epidermal growth factor receptor (EGFR) to drive oncogenic signaling promoting tumor survival and growth. In metabolic disorders like diabetes alterations in GIV’s signaling pathways contribute to insulin resistance. Investigations into these interactions highlight the potential for targeting GIV therapeutically using inhibitors like DUB inhibitors and PR-619.

Product protocols

Publications (11)

Recent publications for all applications. Explore the full list and refine your search

Theranostics 15:4526-4549 PubMed40225577

2025

Targeting USP11 counteracts -associated interstitial lung disease in hiPSCs-derived alveolar organoids and in vivo models.

Applications

Unspecified application

Species

Unspecified reactive species

Janardhan Keshav Karapurkar,Sripriya Rajkumar,Ji-Hye Jung,Ji-Young Kim,Girish Birappa,D A Ayush Gowda,Jencia Carminha Colaco,Bharathi Suresh,Jung-Yun Choi,Sang Hyeon Woo,Won-Jun Jo,Jong-Hee Lee,Kye-Seong Kim,Seok-Ho Hong,Suresh Ramakrishna

Cellular and molecular life sciences : CMLS 81:145 PubMed38498222

2024

USP28 promotes tumorigenesis and cisplatin resistance by deubiquitinating MAST1 protein in cancer cells.

Applications

Unspecified application

Species

Unspecified reactive species

Janardhan Keshav Karapurkar,Jencia Carminha Colaco,Bharathi Suresh,Apoorvi Tyagi,Sang Hyeon Woo,Won-Jun Jo,Nare Ko,Vijai Singh,Seok-Ho Hong,Seung Jun Oh,Kye-Seong Kim,Suresh Ramakrishna

Journal of experimental & clinical cancer research : CR 42:121 PubMed37170124

2023

CRISPR/Cas9-based genome-wide screening of the deubiquitinase subfamily identifies USP3 as a protein stabilizer of REST blocking neuronal differentiation and promotes neuroblastoma tumorigenesis.

Applications

Unspecified application

Species

Unspecified reactive species

Janardhan Keshav Karapurkar,Min-Seong Kim,Jencia Carminha Colaco,Bharathi Suresh,Neha Sarodaya,Dong-Ho Kim,Chang-Hwan Park,Seok-Ho Hong,Kye-Seong Kim,Suresh Ramakrishna

Theranostics 12:5949-5970 PubMed35966591

2022

CRISPR/Cas9-based genome-wide screening for deubiquitinase subfamily identifies USP1 regulating MAST1-driven cisplatin-resistance in cancer cells.

Applications

Unspecified application

Species

Unspecified reactive species

Apoorvi Tyagi,Kamini Kaushal,Arun Pandian Chandrasekaran,Neha Sarodaya,Soumyadip Das,Chang-Hwan Park,Seok-Ho Hong,Kye-Seong Kim,Suresh Ramakrishna

Cell reports 31:107783 PubMed32579915

2020

Precise Temporal Regulation of Post-transcriptional Repressors Is Required for an Orderly Drosophila Maternal-to-Zygotic Transition.

Applications

Unspecified application

Species

Unspecified reactive species

Wen Xi Cao,Sarah Kabelitz,Meera Gupta,Eyan Yeung,Sichun Lin,Christiane Rammelt,Christian Ihling,Filip Pekovic,Timothy C H Low,Najeeb U Siddiqui,Matthew H K Cheng,Stephane Angers,Craig A Smibert,Martin Wühr,Elmar Wahle,Howard D Lipshitz

Cell death and differentiation 27:3004-3020 PubMed32415280

2020

Genome-scale screening of deubiquitinase subfamily identifies USP3 as a stabilizer of Cdc25A regulating cell cycle in cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Soumyadip Das,Arun Pandian Chandrasekaran,Bharathi Suresh,Saba Haq,Jae-Hyeok Kang,Su-Jae Lee,Jaewon Kim,Jaesang Kim,Sanghyuk Lee,Hyongbum Henry Kim,Kye-Seong Kim,Suresh Ramakrishna

eLife 8: PubMed31589140

2019

Dynamic ubiquitination determines transcriptional activity of the plant immune coactivator NPR1.

Applications

Unspecified application

Species

Unspecified reactive species

Michael J Skelly,James J Furniss,Heather Grey,Ka-Wing Wong,Steven H Spoel

Oncogene 38:6051-6064 PubMed31292489

2019

Anti-apoptotic effect by the suppression of IRF1 as a downstream of Wnt/β-catenin signaling in colorectal cancer cells.

Applications

Unspecified application

Species

Unspecified reactive species

Tomoyuki Ohsugi,Kiyoshi Yamaguchi,Chi Zhu,Tsuneo Ikenoue,Kiyoko Takane,Masaru Shinozaki,Giichiro Tsurita,Hideaki Yano,Yoichi Furukawa

Nature communications 9:524 PubMed29410401

2018

Ub-ProT reveals global length and composition of protein ubiquitylation in cells.

Applications

Unspecified application

Species

Unspecified reactive species

Hikaru Tsuchiya,Daocharad Burana,Fumiaki Ohtake,Naoko Arai,Ai Kaiho,Masayuki Komada,Keiji Tanaka,Yasushi Saeki

Molecular cell 66:622-634.e8 PubMed28575658

2017

RFWD3-Mediated Ubiquitination Promotes Timely Removal of Both RPA and RAD51 from DNA Damage Sites to Facilitate Homologous Recombination.

Applications

Unspecified application

Species

Unspecified reactive species

Shojiro Inano,Koichi Sato,Yoko Katsuki,Wataru Kobayashi,Hiroki Tanaka,Kazuhiro Nakajima,Shinichiro Nakada,Hiroyuki Miyoshi,Kerstin Knies,Akifumi Takaori-Kondo,Detlev Schindler,Masamichi Ishiai,Hitoshi Kurumizaka,Minoru Takata
View all publications

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