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Z-Tau-Asn-Phe-Phe-OCH3 is a synthetic peptide consisting of six amino acids: Z-Tau, Asn (asparagine), Phe (phenylalanine), Phe, and OCH3 (methoxy group). Z-Tau-Asn-Phe-Phe-OCH3 is a derivative of the naturally occurring peptide sequence found in the tau protein, which is associated with neurodegenerative diseases such as Alzheimer's. The Z-Tau prefix indicates that the N-terminal amino acid is blocked by a benzyloxycarbonyl (Z) group, protecting it from unwanted reactions. The presence of two phenylalanine residues in the sequence contributes to the hydrophobic nature of the peptide, which may play a role in its potential aggregation and interaction with other proteins. The methoxy group at the C-terminus provides additional stability and solubility properties to the molecule. This synthetic peptide is often used in research to study the mechanisms of protein aggregation and to develop potential therapeutic strategies for tauopathies.

98154-88-2

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98154-88-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 98154-88-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 9,8,1,5 and 4 respectively; the second part has 2 digits, 8 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 98154-88:
(7*9)+(6*8)+(5*1)+(4*5)+(3*4)+(2*8)+(1*8)=172
172 % 10 = 2
So 98154-88-2 is a valid CAS Registry Number.

98154-88-2Downstream Products

98154-88-2Relevant academic research and scientific papers

New analogs of somatostatin with unexpected effects in vivo on insulin basal secretion in the rat

Diaz,Cazaubon,Demarne,et al.

, p. 219 - 227 (2007/10/02)

Twenty analogs of somatostatin were synthesized by the alternating solution/solid-phase procedure. The peptide analogs contained taurine, aza-alanine, or D-amino acids as well as multiple deletions. The aim of this study was to obtain analogs that would selectively inhibit insulin or glucagon release. The biological activities were evaluated in vivo in the rat by measuring the effects of the modified somatostatin molecules on basal secretion of insulin and glucagon in the portal vein. Although some selective analogs were found, a few of them having a taurine or an aza-alanine residue in their structure caused a significant increase of insulin secretion. This unexpected phenomenon, for which we do not have an explanation at present, is under investigation.

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