296270-92-3

Basic information

• Product Name: Carbamic acid, [trans-4-[[(1,1-dimethylethoxy)carbonyl]amino]cyclohexyl]-, phenylmethyl ester
• Synonyms: Carbamic acid, [trans-4-[[(1,1-dimethylethoxy)carbonyl]amino]cyclohexyl]-, phenylmethyl ester
• CAS NO: 296270-92-3
• Molecular Formula: C₁₉H₂₈N₂O₄
• Molecular Weight: 348.43662
• Mol File: 296270-92-3.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: Carbamic acid, [trans-4-[[(1,1-dimethylethoxy)carbonyl]amino]cyclohexyl]-, phenylmethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, [trans-4-[[(1,1-dimethylethoxy)carbonyl]amino]cyclohexyl]-, phenylmethyl ester(296270-92-3)
• EPA Substance Registry System: Carbamic acid, [trans-4-[[(1,1-dimethylethoxy)carbonyl]amino]cyclohexyl]-, phenylmethyl ester(296270-92-3)

Safety Data

• Hazardous Substances Data: 296270-92-3(Hazardous Substances Data)

Upstream product

• 501-53-1 benzyl chloroformate 
• 177906-48-8 trans-N-Boc-1,4-cyclohexanediamine 

Downstream Products

• 149423-77-8 benzyl ((trans)-4-aminocyclohexyl)carbamate 

Relevant articles and documents

Binuclear NiII-DpaTyr complex as a high affinity probe for an oligo-aspartate tag tethered to proteins

A complementary recognition pair of a short-peptide tag and a small molecular probe is a versatile molecular tool for protein detection, handling, and purification, and so forth. In this manuscript, we report that the binuclear NiII-DpaTyr (DpaTyr = bis((dipicolylamino)methyl)-tyrosine) complex serves as a strong binding probe for an oligo-aspartate tag tethered to a protein. Among various binuclear metal complexes of M-DpaTyr (M = Zn II, NiII, MnII, CuII, Cd II, CoIII, and FeIII), we have found that NiII-DpaTyr (1-2NiII) displays a strongbinding affinity (apparent binding constant: Kapp≈105M-1) for an oligo-aspartate peptide under neutral aqueous conditions (50 mM HEPES, 100 mM NaCl, pH 7.2). Detailed isothermal-titration calorimetry (ITC) studies reveal that the tri-aspartate D3-tag (DDD) is an optimal sequence recognized by 1-2NiII in a 1:1 binding stoichiometry. On the other hand, other metal complexes of DpaTyr, except for NiII-and ZnII- DpaTyr, show a negligible binding affinity for the oligo-aspartate peptide. The binding affinity was greatly enhanced in the pair between the dimer of Ni II-DpaTyr and the repeated D3 tag peptide (D3x2), such as DDDXXDDD, on the basis of the multivalent coordination interaction between them. Most notably, a remarkably high-binding affinity (Kapp 10 9M-1) was achieved between the NiII-DpaTyr dimer 4-4NiII and the D3 x 2 tag peptide (DDDNGDDD). This affinity is ≈fold stronger than that observed in the binding pair of the Zn II-DpaTyr (4-4ZnII) and the D4x2 tag (DDDDGDDDD), a useful tagprobe pair previously reported by us. The recognition pair of the Ni II-DpaTyr probe and the D3 x 2 tag can also work effectively on a protein surface, that is, 4-4NiII is strongly bound to the FKBP12 protein tethered with the D3 x 2 tag (DDDNGDDD) with a large Kapp value of 5 x 108 m-1. Taking advantage of the strong-binding affinity, this pair was successfully applied to the selective inactivation of the tagfused (β-galactosidase by using the chromophore-assisted light inactivation (CALI) technique under crude conditions, such as cell lysate.