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PTP Inhibitor I
CAS No. 2491-38-5
PTP Inhibitor I( —— )
Catalog No. M18306 CAS No. 2491-38-5
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.
Purity : >98% (HPLC)
COA
Datasheet
HNMR
HPLC
MSDS
Handing Instructions
| Size | Price / USD | Stock | Quantity |
| 100MG | Get Quote | In Stock |
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| 200MG | Get Quote | In Stock |
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| 500MG | Get Quote | In Stock |
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| 1G | 27 | In Stock |
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Biological Information
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Product NamePTP Inhibitor I
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NoteResearch use only, not for human use.
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Brief DescriptionPTP 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.
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DescriptionPTP 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.
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In Vitro——
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In Vivo——
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Synonyms——
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PathwayOthers
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TargetOther Targets
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RecptorPTP
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Research Area——
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Indication——
Chemical Information
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CAS Number2491-38-5
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Formula Weight215.04
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Molecular FormulaC8H7BrO2
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Purity>98% (HPLC)
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SolubilityIn Vitro:?DMSO : 250 mg/mL (1162.57 mM)
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SMILESOc1ccc(cc1)C(=O)CBr
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Chemical Name——
Shipping & Storage Information
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Storage(-20℃)
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ShippingWith Ice Pack
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Stability≥ 2 years
Reference
1. Arabaci, G., et al. αHaloacetophenone derivatives as photoreversible covalent inhibitors of protein tyrosine phosphatases. Journal of the American Chemical Society 121(21), 5085-5086 (1999).
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