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BOC-CYS(DPM)-OH is a chemical compound categorized as a protected amino acid, specifically cysteine. It is widely utilized in the realms of biochemistry and peptide synthesis. The BOC (tert-butyloxycarbonyl) group serves as a protective agent for the amino group, while the DPM (diphenylmethyl) group shields the sulfur atom in the cysteine. The presence of the OH (hydroxyl) group is also a key feature. These elements collectively render BOC-CYS(DPM)-OH a vital component in biochemical research and pharmaceutical development, particularly in the synthesis of polypeptides or proteins. BOC-CYS(DPM)-OH is engineered to withstand laboratory conditions until the protective groups are deliberately removed at a subsequent stage in the synthesis process.

21947-97-7

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21947-97-7 Usage

Uses

Used in Biochemistry Research:
BOC-CYS(DPM)-OH is employed as a protected amino acid in biochemistry research, facilitating the synthesis of complex polypeptides and proteins. Its protective groups ensure that the cysteine residue remains stable and unreactive until the desired point in the synthesis process.
Used in Peptide Synthesis:
In the field of peptide synthesis, BOC-CYS(DPM)-OH is used as a building block for creating larger polypeptide chains. The protection of the amino and sulfur groups by BOC and DPM, respectively, allows for controlled reactions and prevents unwanted side reactions during the synthesis process.
Used in Drug Manufacturing:
BOC-CYS(DPM)-OH is utilized in the pharmaceutical industry as a key component in the synthesis of therapeutic peptides and proteins. Its protective groups enable the production of drugs with specific amino acid sequences, which can be crucial for their biological activity and therapeutic efficacy.
Used in the Synthesis of Biologically Active Molecules:
BOC-CYS(DPM)-OH is used as a precursor in the synthesis of biologically active molecules, such as enzymes, hormones, and antibodies. The protection of the cysteine residue ensures that these molecules maintain their structural integrity and biological function throughout the synthesis process.

Check Digit Verification of cas no

The CAS Registry Mumber 21947-97-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,1,9,4 and 7 respectively; the second part has 2 digits, 9 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 21947-97:
(7*2)+(6*1)+(5*9)+(4*4)+(3*7)+(2*9)+(1*7)=127
127 % 10 = 7
So 21947-97-7 is a valid CAS Registry Number.

21947-97-7SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 16, 2017

Revision Date: Aug 16, 2017

1.Identification

1.1 GHS Product identifier

Product name Boc-S-diphenylmethyl-L-cysteine

1.2 Other means of identification

Product number -
Other names (2R)-3-benzhydrylsulfanyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid

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:21947-97-7 SDS

21947-97-7Relevant academic research and scientific papers

Synthesis of a Protected Cyclic Disulphide Octapeptide A6-13 of the (Ala12)-Sheep Insulin-A-Chain

Kaufmann, Klaus-Dieter,Nieke, Eva-Maria

, p. 665 - 674 (2007/10/02)

The synthesis of a protected (Ala12)-sheep insulin-A-chain octapeptide with a 6,11-disulphide ring using the combination of A6,11-S-trityl/A7-S-diphenylmethyl thiol protecting groups is described.For the formation of the cyclic disulphide octapeptide 2 the linear octapeptide, Boc-Cys(Trt)Cys(Dpm)AlaGlyValCys(Trt)Ala-Leu-OH (1), is prepared by a 4 + 4- as well as a 3 + 2 + 3-fragment condensation scheme followed by treatment with iodine in methanol.Most of the peptide coupling reactions were performed using the azide technique obtaining the intermediate peptide fragments in good yields.For the characterization of the cyclic disulphide peptide 2 the 13C-n.m.r.-spectroscopy was used in combination with other usual methods.

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