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24032-35-7

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24032-35-7 Usage

Chemical Properties

Off-white to yellowish crystalline powder

Check Digit Verification of cas no

The CAS Registry Mumber 24032-35-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,4,0,3 and 2 respectively; the second part has 2 digits, 3 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 24032-35:
(7*2)+(6*4)+(5*0)+(4*3)+(3*2)+(2*3)+(1*5)=67
67 % 10 = 7
So 24032-35-7 is a valid CAS Registry Number.
InChI:InChI=1/C11H13N3O5/c12-9(5-6-10(15)16)11(17)13-7-1-3-8(4-2-7)14(18)19/h1-4,9H,5-6,12H2,(H,13,17)(H,15,16)/t9-/m0/s1

24032-35-7SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 18, 2017

Revision Date: Aug 18, 2017

1.Identification

1.1 GHS Product identifier

Product name H-GLU-PNA

1.2 Other means of identification

Product number -
Other names GLUTAMIC ACID-PNA

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:24032-35-7 SDS

24032-35-7Upstream product

24032-35-7Relevant articles and documents

Purification and Some Properties of a Protease from the Sarcocarp of Musk Melon Fruit

Kaneda, Makoto,Yonezawa, Hiroo,Uchikoba, Tetsuya

, p. 2100 - 2102 (2007/10/03)

A protease has been purified from sarcocarp of musk melon.Cucumis melo ssp. melo var. reticulatus Naud.Earl's Favourite.The protease was mostly present in the placenta part of the fruit and next in the inside mesocarp.The molecular mass of the enzyme was estimated to be about 62 kDa on SDS-PAGE.The enzyme had a carbohydrate moiety.The optimum pH of the enzyme was 11 at 35 deg C using casein as a substrate.The enzyme was stable between pH 6 and 11.The enzyme was strongly inhibited by diisopropyl fluorophosphate, but was not inhibited by EDTA or cysteine protease inhibitors.From the digestion of Ala-Ala-Pro-X-pNA (X = Phe, Leu, Val, Ala, Gly, Lys, Glu, Pro, and diaminopropionic acid (Dap) substrates the specificity of the protease was found to be approximately broad, but the preferential cleavage sites were C-terminal sites of h)drophobic or acidic amino acid residues at P1 position.It was proved that the enzymatic properties of musk melon protease are similar to those of cucumisin .The enzvme was not inhibited by typical proteinous inhibitors such as STI or ovomucoid.Therefore, this enzyme seems to be a useful protease for the food industries. - Keywords: Cucumis melo; Cucurbitaceae; musk melon; plant protease; serine protease.

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