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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:
893449-38-2
Peso molecular:
485.21
MDL number:
MFCD11045303
UNSPSC Code:
12352200
PubChem Substance ID:
329820016
NACRES:
NA.77

Quality Level

100

assay

≥98% (HPLC)

form

solid

storage condition

protect from light

color

yellow

solubility

DMSO: >10 mg/mL
H2O: <2 mg/mL

storage temp.

−20°C

SMILES string

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+

InChI key

HXNBAOLVPAWYLT-OVCLIPMQSA-N

Application

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

Biochem/physiol Actions

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.

Features and Benefits

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.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

ppe

dust mask type N95 (US), Eyeshields, Gloves

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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
Magnus Aassved Hjort et al.
Experimental hematology & oncology, 7, 8-8 (2018-04-14)
Phosphatase of regenerating liver-3 (PRL-3) is implicated in oncogenesis of hematological and solid cancers. PRL-3 expression increases metastatic potential, invasiveness and is associated with poor prognosis. With this study, we aimed to show a possible oncogenic role of PRL-3 in
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
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
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
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Artículos

Phosphoprotein Phosphatases (Tyrosine)

Protein tyrosine phosphatases' catalytic mechanism involves transient phosphorylation.

Phosphoprotein Phosphatases (Tyrosine)

Protein tyrosine phosphatases' catalytic mechanism involves transient phosphorylation.

Phosphoprotein Phosphatases (Tyrosine)

Protein tyrosine phosphatases' catalytic mechanism involves transient phosphorylation.

Phosphoprotein Phosphatases (Tyrosine)

Protein tyrosine phosphatases' catalytic mechanism involves transient phosphorylation.

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