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3-Methylhistidine is a post-translational modification product of histidine, an amino acid found in proteins. It is formed through the demethylation of 1-methylhistidine and 3-methylhistidine, which are derived from the methylation of histidine residues in proteins. This chemical modification plays a significant role in various biological processes, including protein turnover and muscle metabolism. 3-Methylhistidine is also of interest in medical research as it can be used as a biomarker for muscle protein breakdown, particularly in conditions such as cachexia and muscular dystrophy. Its measurement in urine or blood can provide insights into the rate of muscle protein degradation, making it a valuable tool in the assessment of muscle wasting disorders and the effectiveness of therapeutic interventions.

7212-31-9

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7212-31-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 7212-31-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,2,1 and 2 respectively; the second part has 2 digits, 3 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 7212-31:
(6*7)+(5*2)+(4*1)+(3*2)+(2*3)+(1*1)=69
69 % 10 = 9
So 7212-31-9 is a valid CAS Registry Number.

7212-31-9Downstream Products

7212-31-9Relevant academic research and scientific papers

Immunomodulatory peptides

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, (2014/12/12)

The invention relates to peptides derivatized with a hydrophilic polymer which, in some embodiments, bind to human FcRn and inhibit binding of the Fc portion of an IgG to an FcRn, thereby modulating serum IgG levels. The disclosed compositions and methods may be used in some embodiments, for example, in treating autoimmune diseases and inflammatory disorders. The invention also relates, in further embodiments, to methods of using and methods of making the peptides of the invention.

Method for the production of amino terminus protected naturally occurring amino acids

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, (2008/06/13)

A method for the production of substantially 100% pure Nα-urethane protected amino acids is disclosed. This method eliminates the formation of di-peptide and tri-peptide contaminants. Reaction of blocking reagents at the carboxylate site on a protected peptide is prevented by the application of labile amino acid esters. Subsequent removal of the ester yields, in ultra-high purity, the Nα-protected amino acid. The substantially 100% pure Nα-urethane protected amino acid are also disclosed.

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