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Z-Leu-Phe-Leu-NH2 is a synthetic tetrapeptide, consisting of four amino acid residues: Leucine (Leu), Phenylalanine (Phe), and two additional Leucine residues. The "Z" group is a protecting group, which is used in peptide synthesis to prevent unwanted side reactions. This peptide is often used as a model compound in studies related to peptide synthesis, protein folding, and drug design. It can also serve as a substrate for various enzymes, such as proteases, and is used to investigate enzyme kinetics and specificity. The sequence of amino acids in Z-Leu-Phe-Leu-NH2 provides a simple yet informative structure for understanding peptide interactions and properties.

79259-43-1

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79259-43-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 79259-43-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,9,2,5 and 9 respectively; the second part has 2 digits, 4 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 79259-43:
(7*7)+(6*9)+(5*2)+(4*5)+(3*9)+(2*4)+(1*3)=171
171 % 10 = 1
So 79259-43-1 is a valid CAS Registry Number.

79259-43-1Downstream Products

79259-43-1Relevant academic research and scientific papers

Peptide Synthesis by Means of Immobilized Enzymes. I. Immobilized α-Chimotripsin

Koennecke, Andreas,Bullerjahn, Ralf,Jakubke, Hans-Dieter

, p. 469 - 482 (2007/10/02)

α-Chymotrypsin covalently bound to silica, enzacryl AA, and enzacryl AH catalyzes peptide bond formation between N-protected dipeptide methyl esters and H-Leu-NH2 with results similar to those with the free enzyme.The influence of water-miscible and water

Model Studies on Papain-Catalyzed Peptide Synthesis in a Biphasic Aqueous-Organic System

Doering, Guenter,Kuhl, Peter,Jakubke, Hans-Dieter

, p. 1165 - 1174 (2007/10/02)

Several model peptides have been synthesized enzymatically using papain as a catalyst in biphasic aqueous-organic systems.The effect of different cosolvents, pH, buffer concentration, and reaction time on the papain-catalyzed synthesis was examined.A comp

Attempts for the Application of Thermitase as a Catalyst for Peptide Bond Formation

Koennecke, Andreas,Jakubke, Hans-Dieter

, p. 1099 - 1102 (2007/10/02)

The utility of thermitase, a thermophilic proteolytic enzyme from Thermoactinomyces vulgaris, as a catalyst for peptide synthesis has been studied using several Nα-benzyloxycarbonyl dipeptide esters as carboxyl components and Leu-NH2 as nucleophile.Couplings were most successfull with substrates containing Met, Leu, Ala, Phe, Tyr in P1-position, and Val, Ala, Pro in P2, whereas the substrates with Val, Ile, Pro in P1 failed to couple. - Keywords: Enzymatic peptide synthesis; Thermitase

α-Chymotrypsin-catalyzed Synthesis of Tripeptide Amides in an Aqueous-Organic Two-phase System

Kuhl, P.,Posselt, Siegrid,Jakubke, H.-D.

, p. 463 - 465 (2007/10/02)

α-Chymotrypsin catalyzes in a biphasic system containing an organic solvent and hydrogencarbonate buffer the reaction of Boc-Leu-Phe-OMe with X-NH2 (X=Leu, Met, Val) forming Boc-tripeptide amides.In the case of X=Leu the addition of ammoniumsulfate is advantageous and allows the use of carboxyl and amino component in equivalent amounts.By the same method Z-protected tripeptide amides can be prepared from Z-X-Phe-OMe (X=Ala, Leu, Val) and Leu-NH2 in good yields.In some case α-chymotrypsin-catalyzed peptide coupling is also possible, if the buffer solution is substituted for crystal water containing sodium carbonate.

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