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Merck

P0108

Sigma-Aldrich

PRL-3 Inhibitor I

≥98% (HPLC), solid

Sinónimos:

5-[[5-bromo-2-[(2-bromophenyl)methoxy]phenyl]methylene]-2-thioxo-4-thiazolidinone, Phosphatase of regenerating liver-3, Inhibitor I

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About This Item

Fórmula empírica (notación de Hill):
C17H11Br2NO2S2
Número de CAS:
Peso molecular:
485.21
Número MDL:
Código UNSPSC:
12352200
ID de la sustancia en PubChem:
NACRES:
NA.77

Nivel de calidad

Análisis

≥98% (HPLC)

formulario

solid

condiciones de almacenamiento

protect from light

color

yellow

solubilidad

DMSO: >10 mg/mL
H2O: <2 mg/mL

temp. de almacenamiento

−20°C

cadena SMILES

Brc1ccc(OCc2ccccc2Br)c(c1)\C=C3\SC(=S)NC3=O

InChI

1S/C17H11Br2NO2S2/c18-12-5-6-14(22-9-10-3-1-2-4-13(10)19)11(7-12)8-15-16(21)20-17(23)24-15/h1-8H,9H2,(H,20,21,23)/b15-8+

Clave InChI

HXNBAOLVPAWYLT-OVCLIPMQSA-N

Aplicación

PRL-3 Inhibitor I has been used as an inhibitor of phosphatase of regenerating liver-3 (PRL-3):
  • to test its effect on classical Hodgkin lymphoma cell survival
  • in the human umbilical vein endothelial cells tube formation assay
  • to test its effect on the migration of neural crest cells

Acciones bioquímicas o fisiológicas

PRL-3 Inhibitor I is a rhodanine derivative with an IC50 value of 0.9 μM against phosphatase of regenerating liver-3 (PRL-3), a nonclassical protein tyrosine phosphatase that has recently been shown to be involved in cancer metastasis. PRL-3 Inhibitor I reduced the invasiveness of B16F10 melanoma cells in a cell based assay.

Características y beneficios

This compound is featured on the Phosphoprotein Phosphatases (Tyrosine) page of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Equipo de protección personal

dust mask type N95 (US), Eyeshields, Gloves


Certificados de análisis (COA)

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Jianliang Xu et al.
PloS one, 6(11), e27165-e27165 (2011-11-11)
Phosphatase of regenerating liver 3 (PRL-3) is known to be overexpressed in many tumors, and its transcript level is high in the vasculature and endothelial cells of malignant tumor tissue. However, the mechanism(s) underlying its enhanced expression and its function
Jin Hee Ahn et al.
Bioorganic & medicinal chemistry letters, 16(11), 2996-2999 (2006-03-15)
A series of rhodanine derivatives was synthesized and evaluated for their ability to inhibit PRL-3. Benzylidene rhodanine derivative showed good biological activity, while compound 5e was the most active in this series exhibiting an IC50 value of 0.9 microM in
E G Garcia et al.
Leukemia, 35(3), 679-690 (2020-07-02)
T-cell acute lymphoblastic leukemia (T-ALL) is an aggressive malignancy of thymocytes and is largely driven by the NOTCH/MYC pathway. Yet, additional oncogenic drivers are required for transformation. Here, we identify protein tyrosine phosphatase type 4 A3 (PRL3) as a collaborating
Ying-Qian Lu et al.
Stem cell research, 34, 101354-101354 (2019-01-06)
The human iPS cell line, hiPS-SPG76 (FJMUi001-A), derived from skin fibroblasts from a 42-year-old male hereditary spastic paraplegia patient carrying compound heterozygous p.P498L (c.1493C > T) and p.R618W (c.1852C > T) mutations in the CAPN1 gene, was generated by non-integrative reprogramming vectors encoding OCT3/4
Jeanette A Johansson et al.
Developmental cell, 54(3), 317-332 (2020-07-12)
Melanocytes, replenished throughout life by melanocyte stem cells (MSCs), play a critical role in pigmentation and melanoma. Here, we reveal a function for the metastasis-associated phosphatase of regenerating liver 3 (PRL3) in MSC regeneration. We show that PRL3 binds to

Artículos

Protein tyrosine phosphatases (PTPs) and related enzymes (more than a hundred coded by the human genome) are more numerous than serine/threonine phosphatases. They belong to four families, three of which possess a conserved cysteine for catalysis and some conserved features of 3-dimensional structure. The catalytic mechanism of these PTPs involves the transient formation of a covalently phosphorylated enzyme.

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