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Chemical structure of CAS 901-47-3

Tosylarginine Methyl Ester

In Stock•Starting at $28 for 1 mg•Purity ≥ 99%
CAS No.901-47-3
MDL No.MFCD01320524
MFC14H22N4O4S
MW342.42
InChI KeyFKMJXALNHKIDOD-LBPRGKRZSA-N
CUSTOM SYNTHESISPRECLINICAL SUPPORT→

Pricing & Availability

Pack SizePurityPriceAvailabilityAction
1 mgTo Be Confirmed$28In Stock
5 mgTo Be Confirmed$50In Stock
10 mg≥99%$80In Stock
25 mgTo Be Confirmed$113In Stock
50 mg≥99%$147In Stock
Custom synthesis and bulk supply options are available upon request.

Product Information

TAMe is an L-arginine ester, specifically methyl L-argininate, in which one hydrogen on the alpha-nitrogen is replaced by a tosyl group. It is a sulfonamide, a methyl ester, and a member of the guanidine class.

CAS No.901-47-3
Product NameTosylarginine Methyl Ester
Heavy Atom Count23Rotatable Bond Count8
Atom Stereo Count1Bond Stereo Count0
HBA5HBD3
TPSA136.870 ŲCharge0
Exact Mass342.13618Complexity651.86
pKa7.130XLogP-0.131

Related Articles

Studies related to this compound and its mechanism of action

Kinetic peculiarities of human tissue kallikrein: 1--substrate activation in the catalyzed hydrolysis of H-D-valyl-L-leucyl-L-arginine 4-nitroanilide and H-D-valyl-L-leucyl-L-lysine 4-nitroanilide; 2--substrate inhibition in the catalyzed hydrolysis of N alpha-p-tosyl-L-arginine methyl ester.

Archives of biochemistry and biophysics • Vol. 400, Issue 1 • 2002
PMID: 11913965DOI: 10.1006/abbi.2002.2764

Variations in biochemical and pharmacological properties of Indian cobra (Naja naja naja) venom due to geographical distribution.

Molecular and cellular biochemistry • Vol. 229, Issue 1-2 • 2002
PMID: 11936852DOI: 10.1023/a:1017972511272

Isolation and characteristics of trypsin from pyloric ceca of the starfish Asterina pectinifera.

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology • Vol. 132, Issue 2 • 2002
PMID: 12031475DOI: 10.1016/s1096-4959(02)00062-3

The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium.

The Journal of biological chemistry • Vol. 276, Issue 35 • 2001
PMID: 11404362DOI: 10.1074/jbc.M104731200

Documentation

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