60254-82-2 Usage
Description
BETA-LIPOTROPIN, FRAGMENT 61-64 is a peptide fragment derived from the protein beta-lipotropin, consisting of the amino acid sequence 61-64. It is believed to have potential effects on appetite regulation, metabolism, pain modulation, and stress response, with possible neuroprotective and anti-inflammatory properties.
Uses
Used in Pharmaceutical Industry:
BETA-LIPOTROPIN, FRAGMENT 61-64 is used as a potential therapeutic agent for conditions such as obesity, chronic pain, and neurodegenerative diseases due to its potential effects on appetite regulation, metabolism, and pain modulation.
Used in Research Applications:
BETA-LIPOTROPIN, FRAGMENT 61-64 is used as a research tool to study the mechanisms of appetite regulation, metabolism, pain modulation, and stress response, as well as its potential neuroprotective and anti-inflammatory properties.
Check Digit Verification of cas no
The CAS Registry Mumber 60254-82-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 6,0,2,5 and 4 respectively; the second part has 2 digits, 8 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 60254-82:
(7*6)+(6*0)+(5*2)+(4*5)+(3*4)+(2*8)+(1*2)=102
102 % 10 = 2
So 60254-82-2 is a valid CAS Registry Number.
InChI:InChI=1/C22H26N4O6/c23-17(10-15-6-8-16(27)9-7-15)21(30)25-12-19(28)24-13-20(29)26-18(22(31)32)11-14-4-2-1-3-5-14/h1-9,17-18,27H,10-13,23H2,(H,24,28)(H,25,30)(H,26,29)(H,31,32)/t17-,18-/m0/s1
60254-82-2Relevant articles and documents
A Facile Synthesis of NODASA-Functionalized Peptide
Dutta, Jyotibon,Chinthakindi, Praveen K.,Arvidsson, Per I.,De La Torre, Beatriz G.,Kruger, Hendrik G.,Govender, Thavendran,Naicker, Tricia,Albericio, Fernando
, p. 1685 - 1688 (2016)
Herein, we report a mild and efficient synthesis of a NODASA-functionalized peptide, which was initiated with a Michael addition reaction between monomethyl fumarate and 1,4,7-triazacyclononane.
SPECIFICITY AND MOLECULAR PROPERTIES OF PENICILLOLYSIN, A METALLOPROTEINASE FROM PENICILLUM CITRINUM
Yamaguchi, Megumi,Hanzawa, Satoshi,Hirano, Ken-Ichi,Yamagata, Youhei,Ichishima, Eiji
, p. 1317 - 1322 (2007/10/02)
The specificity and mode of action of penicillolysin, a metalloproteinase from Penicillum citrinum, were investigated with several bioactive-oligopeptides.The enzyme showed a high affinity toward the Pro-X (X = Gln, Lys, Leu or Arg) bonds of substance P, dynorphin A (1-13), neurotensin and chicken brain pentapeptide, and the R-R bonds in dynorphin A and neurotensin.Preferential cleavages of bonds by the enzyme with hydrophobic amino acid residues at the P1 position were observed on the peptides used.The specificity of penicillolysin differs from that of other metallopropteinases.The Mr and pI were determined as 18000 and 9.6, respectively.The first 50 amino acids in the N-terminal region were TKETCSNASRKSALEKALSNTVKLANAAATAARSGSASKFSEYEKTTSSS.CD spectra on the hollo- and apo-enzymes of penicillolysin were studied.
