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130878-68-1

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130878-68-1 Usage

Chemical Properties

White to off-white powder

Uses

N-Fmoc-L-valine N-succinimidyl ester is useful for solid phase peptide synthesis techniques.

Check Digit Verification of cas no

The CAS Registry Mumber 130878-68-1 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,3,0,8,7 and 8 respectively; the second part has 2 digits, 6 and 8 respectively.
Calculate Digit Verification of CAS Registry Number 130878-68:
(8*1)+(7*3)+(6*0)+(5*8)+(4*7)+(3*8)+(2*6)+(1*8)=141
141 % 10 = 1
So 130878-68-1 is a valid CAS Registry Number.
InChI:InChI=1/C24H24N2O6/c1-14(2)22(23(29)32-26-20(27)11-12-21(26)28)25-24(30)31-13-19-17-9-5-3-7-15(17)16-8-4-6-10-18(16)19/h3-10,14,19,22H,11-13H2,1-2H3,(H,25,30)/t22-/m0/s1

130878-68-1 Well-known Company Product Price

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  • Alfa Aesar

  • (H66946)  N-Fmoc-L-valine N-succinimidyl ester, 95%   

  • 130878-68-1

  • 5g

  • 470.0CNY

  • Detail
  • Alfa Aesar

  • (H66946)  N-Fmoc-L-valine N-succinimidyl ester, 95%   

  • 130878-68-1

  • 25g

  • 1940.0CNY

  • Detail

130878-68-1SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name (2,5-dioxopyrrolidin-1-yl) 2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-methylbutanoate

1.2 Other means of identification

Product number -
Other names (S)-2,5-dioxopyrrolidin-1-yl 2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-3-methylbutanoate

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:130878-68-1 SDS

130878-68-1Relevant articles and documents

Aldehyde capture ligation for synthesis of native peptide bonds

Raj, Monika,Wu, Huabin,Blosser, Sarah L.,Vittoria, Marc A.,Arora, Paramjit S.

, p. 6932 - 6940 (2015)

Chemoselective reactions for amide bond formation have transformed the ability to access synthetic proteins and other bioconjugates through ligation of fragments. In these ligations, amide bond formation is accelerated by transient enforcement of an intramolecular reaction between the carboxyl and the amine termini of two fragments. Building on this principle, we introduce an aldehyde capture ligation that parlays the high chemoselective reactivity of aldehydes and amines to enforce amide bond formation between amino acid residues and peptides that are difficult to ligate by existing technologies.

Isostearyl Mixed Anhydrides for the Preparation of N-Methylated Peptides Using C-Terminally Unprotected N-Methylamino Acids

Cary, Douglas R.,Handa, Michiharu,Kobayashi, Yutaka,Kurasaki, Haruaki,Masuya, Keiichi,Matsuda, Ayumu,Matsumoto, Masatoshi,Morimoto, Koki,Nagaya, Akihiro,Nishizawa, Naoki,Taguri, Tomonori,Takeuchi, Hisayuki

, p. 8039 - 8043 (2020)

Sustainable and efficient manufacturing methods for N-methylated peptides remain underexplored despite growing interest in therapeutic N-methylated peptides within the pharmaceutical industry. A methodology for the coupling of C-terminally unprotected N-methylamino acids mediated by an isostearic acid halide (ISTAX) and silylating reagent has been developed. This approach allows for the coupling of a wide variety of amino acids and peptides in high yields under mild conditions without the need for a C-terminal deprotection step in the process of C-terminal elongation. These advantages make this a useful synthetic method for the production of peptide therapeutics and diagnostics containing N-methylamino acids.

Hydrogelation and self-assembly of Fmoc-tripeptides: Unexpected influence of sequence on self-assembled fibril structure, and hydrogel modulus and anisotropy

Cheng,Castelletto,Moulton,Newby,Hamley

, p. 4990 - 4998 (2010)

The self-assembly and hydrogelation properties of two Fmoc-tripeptides [Fmoc = N-(fluorenyl-9-methoxycarbonyl)] are investigated, in borate buffer and other basic solutions. A remarkable difference in self-assembly properties is observed comparing Fmoc-VLK(Boc) with Fmoc-K(Boc)LV, both containing K protected by Nε-tert-butyloxycarbonate (Boc). In borate buffer, the former peptide forms highly anisotropic fibrils which show local alignment, and the hydrogels show flow-aligning properties. In contrast, Fmoc-K(Boc)LV forms highly branched fibrils that produce isotropic hydrogels with a much higher modulus (G′ > 104 Pa), and lower concentration for hydrogel formation. The distinct self-assembled structures are ascribed to conformational differences, as revealed by secondary structure probes (CD, FTIR, Raman spectroscopy) and X-ray diffraction. Fmoc-VLK(Boc) forms well-defined β-sheets with a cross-β X-ray diffraction pattern, whereas Fmoc-KLV(Boc) forms unoriented assemblies with multiple stacked sheets. Interchange of the K and V residues when inverting the tripeptide sequence thus leads to substantial differences in self-assembled structures, suggesting a promising approach to control hydrogel properties.

Engineering Enzyme-Cleavable Oligonucleotides by Automated Solid-Phase Incorporation of Cathepsin B Sensitive Dipeptide Linkers

Jin, Cheng,EI-Sagheer, Afaf H.,Li, Siqi,Vallis, Katherine A.,Tan, Weihong,Brown, Tom

supporting information, (2022/02/17)

Oligonucleotides containing cleavable linkers have emerged as versatile tools to achieve stimulus-responsive and site-specific cleavage of DNA. However, the limitations of previously reported cleavable linkers including photolabile and disulfide linkers have restricted their applications in vivo. Inspired by the cathepsin B-sensitive dipeptide linkers in antibody–drug conjugates (ADCs) such as Adcetris, we have developed Val-Ala-02 and Val-Ala-Chalcone phosphoramidites for the automated synthesis of enzyme-cleavable oligonucleotides. Cathepsin B digests Val-Ala-02 and Val-Ala-Chalcone linkers efficiently, enabling cleavage of oligonucleotides into two components or release of small-molecule payloads. Based on the prior success of dipeptide linkers in ADCs, we believe that these dipeptide linker phosphoramidites will promote new clinical applications of therapeutic oligonucleotides.

ANTIBODY-DRUG CONJUGATE

-

Page/Page column 55-56; 58-59, (2021/10/22)

Provided herein is an antibody-drug conjugate (ADC) especially a PEGylated mono or bispecific antibody-drug conjugate (BsADC) prepared with site-specific conjugation to provide homogeneous conjugate with high potency and low toxicity. It also relates to a

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