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Benzenepropanamide, a-amino-4-(phenylmethoxy)-, (S)- is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

73504-43-5

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73504-43-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 73504-43-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 7,3,5,0 and 4 respectively; the second part has 2 digits, 4 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 73504-43:
(7*7)+(6*3)+(5*5)+(4*0)+(3*4)+(2*4)+(1*3)=115
115 % 10 = 5
So 73504-43-5 is a valid CAS Registry Number.

73504-43-5Relevant academic research and scientific papers

Mn(II) Complex of Lipophilic Group-Modified Ethylenediaminetetraacetic Acid (EDTA) as a New Hepatobiliary MRI Contrast Agent

Chen, Keyu,Cheng, Tao,Li, Pan,Shen, Chengyi,Wu, Changqiang,Xia, Qian,Xia, Zhiyang,Xiao, Bin,Zhang, Xiaoming,Zhong, Lei,Zhu, Chunrong,Zhu, Jiang

, p. 9182 - 9192 (2021)

Liver-specific contrast agents (CAs) can improve the Magnetic resonance imaging (MRI) detection of focal and diffuse liver lesions by increasing the lesion-to-liver contrast. A novel Mn(II) complex, Mn-BnO-TyrEDTA, with a lipophilic group-modified ethylenediaminetetraacetic acid (EDTA) structure as a ligand to regulate its behavior in vivo, is superior to Gd-EOB-DTPA in terms of a liver-specific MRI contrast agent. An MRI study on mice demonstrated that Mn-BnO-TyrEDTA can be rapidly taken up by hepatocytes with a combination of hepatobiliary and renal clearance pathways. Bromosulfophthalein (BSP) inhibition imaging, biodistribution, and cellular uptake studies confirmed that the mechanism of hepatic targeting of Mn-BnO-TyrEDTA is the hepatic uptake of the amphiphilic anion contrast agent mediated by organic anion transporting polypeptides (OATPs) expressed by functional hepatocytes.

Dipeptide nitrile inhibitors of cathepsin K

Altmann, Eva,Aichholz, Reiner,Betschart, Claudia,Buhl, Thomas,Green, Jonathan,Lattmann, Rene,Missbach, Martin

, p. 2549 - 2554 (2007/10/03)

A series of dipeptidyl nitriles as inhibitors of cathepsin K have been explored starting from lead structure 1 (Cbz-Leu-NH-CH2-CN, IC 50 = 39 nM). Attachment of non-natural amino acid side chains in P1 and modification of the P3 subu

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