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CYS-TYR-PHE-GLN-ASN-CYS-PRO-ARG is a peptide composed of eight amino acids, starting with cysteine (CYS) and ending with arginine (ARG), with tyrosine (TYR), phenylalanine (PHE), glutamine (GLN), asparagine (ASN), and proline (PRO) in between. This arrangement and combination of amino acids are essential for various biological functions, including protein synthesis, energy production, and hormone regulation, and may have specific effects on cellular processes and regulation of physiological functions.

37552-33-3

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37552-33-3 Usage

Uses

Used in Pharmaceutical Industry:
CYS-TYR-PHE-GLN-ASN-CYS-PRO-ARG is used as a therapeutic agent for its potential role in regulating various physiological functions. The specific arrangement of amino acids in this peptide may contribute to its efficacy in targeting and modulating cellular processes, making it a promising candidate for the development of new drugs and therapies.
Used in Nutritional Supplements:
CYS-TYR-PHE-GLN-ASN-CYS-PRO-ARG is used as a nutritional supplement to support protein synthesis, energy production, and hormone regulation in the body. The essential amino acids present in this peptide can help maintain optimal health and support various biological functions.
Used in Cosmetic Industry:
CYS-TYR-PHE-GLN-ASN-CYS-PRO-ARG is used as an ingredient in cosmetic products for its potential benefits in promoting skin health and regeneration. The amino acids present in this peptide may contribute to the maintenance of collagen and elastin, supporting the skin's structure and appearance.
Used in Research and Development:
CYS-TYR-PHE-GLN-ASN-CYS-PRO-ARG is used in research and development for studying the effects of specific amino acid sequences on cellular processes and physiological functions. This peptide can serve as a valuable tool for understanding the mechanisms of action and potential applications in various fields, including medicine, nutrition, and cosmetics.

Check Digit Verification of cas no

The CAS Registry Mumber 37552-33-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,7,5,5 and 2 respectively; the second part has 2 digits, 3 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 37552-33:
(7*3)+(6*7)+(5*5)+(4*5)+(3*2)+(2*3)+(1*3)=123
123 % 10 = 3
So 37552-33-3 is a valid CAS Registry Number.
InChI:InChI=1/C44H61N13O12S2/c45-26-21-70-71-22-32(42(67)57-17-5-9-33(57)41(66)52-28(43(68)69)8-4-16-50-44(48)49)56-40(65)31(20-35(47)60)55-37(62)27(14-15-34(46)59)51-38(63)30(18-23-6-2-1-3-7-23)54-39(64)29(53-36(26)61)19-24-10-12-25(58)13-11-24/h1-3,6-7,10-13,26-33,58H,4-5,8-9,14-22,45H2,(H2,46,59)(H2,47,60)(H,51,63)(H,52,66)(H,53,61)(H,54,64)(H,55,62)(H,56,65)(H,68,69)(H4,48,49,50)/t26-,27-,28-,29-,30+,31-,32?,33?/m0/s1

37552-33-3SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name A Vasopressin Desglycinamide

1.2 Other means of identification

Product number -
Other names DES-GLY-NH2(9),[ARG8]-VASOPRESSIN

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:37552-33-3 SDS

37552-33-3Upstream product

37552-33-3Downstream Products

37552-33-3Relevant academic research and scientific papers

C-terminal deletions in agonistic and antagonistic analogues of vasopressin that improve their specificities for antidiuretic (V2) and vasopressor (V1) receptors

Manning,Misicka,Olma,Klis,Bankowski,Nawrocka,Kruszynski,Kolodziejczyk,Cheng,Seto,Wo,Sawyer

, p. 2245 - 2252 (2007/10/02)

We report the solid-phase synthesis of 12 desGly and 12 desGly(NH2) analogues of arginine-vasopressin (AVP), two highly selective antidiuretic (V2) agonists, four vasopressor (V1) antagonists, and five V2/V1 antagonists. The parent AVP agonists are (1) AVP, (2) 1-deamino[8-D-arginine]vasopressin (dDAVP), and (3) its 4-valine analogue, dVDAVP. The parent V1 antagonists are (4) [1-(β-mercapto-β,β-pentamethylenepropionic acid)]arginine-vasopressin (d(CH2)5AVP), (5) d(CH2)5VDAVP, (6) [1-deaminopenicillamine,4-valine,8-D-arginine]vasopressin (dPVDAVP), and (7) d(CH2)5[Tyr(Me)]AVP. The parent V2/V1 antagonists are (8) d(CH2)5[D-Phe2,Ile4]AVP, (9) d(CH2)5[D-Phe2]VAVP, (10) d(CH2)5[D-Tyr(Et)2]VAVP, (11) d(CH2)5[Tyr(Et2]VAVP, and (12) d(CH2)5[D-Ile2,Ile4]AVP. All 24 analogues were tested for agonistic and antagonistic activities in in vivo rat vasopressor and rat antidiuretic assays. The desGly and desGly(NH2) analogues of 1-3 are either weak partial agonists or weak antagonists of the V1 responses to AVP. Except for desGly(NH2)AVP, which is a weak V2 agonist, the remaining desGly and desGly(NH2) analogues of 1-3 exhibit substantial V2 agonism and are thus highly selective V2 agonists. With antidiuretic activity of 321 units/mg, a resynthesized desGly(NH2)dVDAVP is equipotent with AVP as a V2 agonist. Thus our previously stated conclusion about the need for C-terminal CONH2 for V2 agonism is no longer valid. The four pairs of desGly/desGly(NH2) analogues of the V1 antagonists (4-7) all retained varying degrees of V1 antagonism and some exhibited striking enhancements in anti-V1/V2 selectivity. Thus the desGly/desGly(NH2) analogues of d(CH2)5Tyr(Me)AVP are highly potent V1 antagonists/weak V2 antagonists with anti-V1/V2 selectivities of 200 and 1200, respectively. The four pairs of desGly/desGly(NH2) analogues of the V2/V1 antagonists (8-11) exhibited enhancements, full retention, or slight diminishment of both V1 and V2 antagonism, with the desGly analogue being usually the more potent of each pair. The desGly and desGly(NH2) analogues of d(CH2)5[D-Ile2,Ile4]AVP (12) exhibited anti-V2/V1 selectivities of 46 and about 440, respectively. These are the most selective V2 antagonists reported to date. Many of these analogues could serve as useful pharmacological tools in studies on the roles of AVP in normal and pathophysiological circumstances.

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