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| | 2-Bromo-4'-hydroxyacetophenone Basic information |
| | 2-Bromo-4'-hydroxyacetophenone Chemical Properties |
| Melting point | 123-126°C | | Boiling point | 338.7±17.0 °C(Predicted) | | density | 1.622±0.06 g/cm3(Predicted) | | storage temp. | Inert atmosphere,2-8°C | | solubility | Chloroform (Slightly), Methanol (Slightly) | | pka | 7.69±0.15(Predicted) | | form | White powder | | color | White to Light Beige | | Sensitive | Lachrymatory | | BRN | 1865388 | | Stability: | Hygroscopic | | CAS DataBase Reference | 2491-38-5(CAS DataBase Reference) | | EPA Substance Registry System | 2-Bromo-4-hydroxyacetophenone (2491-38-5) |
| Hazard Codes | C,Xn | | Risk Statements | 22-36 | | Safety Statements | 26 | | RIDADR | 1760 | | WGK Germany | 1 | | RTECS | AM5982000 | | Hazard Note | Corrosive/Lachrymatory/Keep Cold | | HazardClass | 8 | | PackingGroup | III | | HS Code | 2914500090 |
| | 2-Bromo-4'-hydroxyacetophenone Usage And Synthesis |
| Description | PTP Inhibitor I is a cell-permeable, protein tyrosine phosphatase (PTP) inhibitor that covalently blocks the catalytic domain of the Src homology region 2 domain-containing phosphatase (SHP-1(ΔSH2)) with a Ki value of 43 μM and PTP1B with a Ki value of 42 μM. SHP-1 and PTP1B both have known roles in regulating insulin signaling as well as myeloid and lymphoid cell differentiation, making inhibitors of these phosphatases of interest in diabetes, cancer, allergy, and inflammation research. | | Chemical Properties | Pale Beige Solid | | Uses | A covalent inhibitor of protein tyrosine phosphatases (PTPs) | | Preparation | Also obtained by reaction of pyridinium hydrobromide perbromide with 4-hydroxyacetophenone in THF at r.t. for 3 h. | | in vitro | in previous study, the corresponding values of ptp inhibitor i against ptp1b were determined to be ki of 42 μm, kinact of 0.57 min-1, and kinact/ki of 1.4*104 m-1 min-1, respectively. this study also showed that α-bromoacetophenone such as ptp inhibitor i could provide an effective, neutral py mimetic inhibitor of ptps. while perturbation of the electronic properties of the phenyl ring did not significantly improve its potency against ptps, attachment of a proper peptidyl moiety to the para position could improve both the potency and the selectivity substantially. in addition, since the covalent ptp inhibitor complex could be cleaved to regenerate the ptp activity photolytically, ptp inhibitor i might provide a novel class of photolytic switch for controlling cellular signaling processes [1]. | | references | [1] arabaci g, yi t, fu h, porter me, beebe kd, pei d. alpha-bromoacetophenone derivatives as neutral protein tyrosine phosphatase inhibitors: structure-activity relationship. bioorg med chem lett. 2002 nov 4;12(21):3047-50. |
| | 2-Bromo-4'-hydroxyacetophenone Preparation Products And Raw materials |
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