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Val-Lys(Z)-OBzl is a tripeptide composed of three amino acids: valine (Val), lysine (Lys), and a lysine derivative with a benzyloxycarbonyl (Z) protecting group, and a benzyl (OBzl) ester at the C-terminus. This specific sequence and modification are often used in peptide synthesis to protect the side chain amino group of lysine and to facilitate the formation of peptide bonds. The benzyloxycarbonyl group is a temporary protecting group that can be removed under specific conditions to expose the free amino group, allowing for further peptide chain elongation or other chemical modifications. The benzyl ester at the C-terminus can also be removed to generate a free carboxyl group, which is important for certain biological activities or further chemical reactions. This tripeptide serves as a building block in the synthesis of larger peptides and proteins, and its protected structure allows for controlled and selective chemical reactions in the laboratory.

77236-15-8

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77236-15-8 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 77236-15-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,7,2,3 and 6 respectively; the second part has 2 digits, 1 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 77236-15:
(7*7)+(6*7)+(5*2)+(4*3)+(3*6)+(2*1)+(1*5)=138
138 % 10 = 8
So 77236-15-8 is a valid CAS Registry Number.

77236-15-8Relevant academic research and scientific papers

Design, synthesis and evaluation of inhibitor of apoptosis protein (IAP) antagonists that are highly selective for the BIR2 domain of XIAP

Ardecky, Robert J.,Welsh, Kate,Finlay, Darren,Lee, Pooi San,González-López, Marcos,Ganji, Santhi Reddy,Ravanan, Palaniyandi,Mace, Peter D.,Riedl, Stefan J.,Vuori, Kristiina,Reed, John C.,Cosford, Nicholas D.P.

, p. 4253 - 4257 (2013/07/26)

We recently reported the systematic ligand-based rational design and synthesis of monovalent Smac mimetics that bind preferentially to the BIR2 domain of the anti-apoptotic protein XIAP. Expanded structure-activity relationship (SAR) studies around these peptidomimetics led to compounds with significantly improved selectivity (>60-fold) for the BIR2 domain versus the BIR3 domain of XIAP. The potent and highly selective IAP antagonist 8q (ML183) sensitized TRAIL-resistant prostate cancer cells to apoptotic cell death, highlighting the merit of this probe compound as a valuable tool to investigate the biology of XIAP.

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