57468-16-3 Usage
Description
SUBSTANCE P (1-4) is a neuropeptide that belongs to the tachykinin family and functions as a neurotransmitter and neuromodulator. It is composed of a chain of four amino acids and is involved in the transmission of pain and inflammatory signals. This neuropeptide is released by nerve cells in the peripheral and central nervous system in response to noxious stimuli and plays a crucial role in mediating the sensation of pain. Furthermore, it has been implicated in the regulation of various physiological processes, such as smooth muscle contraction, blood vessel dilation, and immune responses. Due to its involvement in pain perception and inflammatory processes, SUBSTANCE P (1-4) is a potential target for the development of novel analgesic and anti-inflammatory medications.
Uses
Used in Pharmaceutical Industry:
SUBSTANCE P (1-4) is used as a target for the development of novel analgesic and anti-inflammatory medications due to its involvement in pain perception and inflammatory processes.
Used in Research and Development:
SUBSTANCE P (1-4) is used as a research tool for studying the mechanisms of pain transmission and the role of neuropeptides in the nervous system. This helps in understanding the underlying pathways and developing potential therapeutic agents for pain and inflammatory disorders.
Check Digit Verification of cas no
The CAS Registry Mumber 57468-16-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,7,4,6 and 8 respectively; the second part has 2 digits, 1 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 57468-16:
(7*5)+(6*7)+(5*4)+(4*6)+(3*8)+(2*1)+(1*6)=153
153 % 10 = 3
So 57468-16-3 is a valid CAS Registry Number.
57468-16-3Relevant articles and documents
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.