Detail of "73731-37-0"

MSDS Download
CAS Number:
73731-37-0
Name:
L-Threonine,N-[(9H-fluoren-9-ylmethoxy)carbonyl]-
Superlist Name:
Fmoc-L-threonine
Molecular Structure:
Formula:
C₁₉H₁₉NO₅
Molecular Weight:
341.37
Synonyms:
N-(9-Fluorenylmethoxycarbonyl)-L-threonine;N-(9-Fluorenylmethoxycarbonyl)threonine;NSC 334300;
Density:
1.327 g/cm³
Melting Point:
115°C (dec.)
Boiling Point:
596.5 °C at 760 mmHg
Flash Point:
314.6 °C
Hazard Symbols:
Xi
Risk Codes:
36/37/38
Safety:
22-24/25-26 Details
particular:
particular

Famous Chemical Enterprises

Livzon
Total
Shell
Dupont
Exxonmobil
Akzonobel
Basf
Bayer
BP

Other Products

Supplier Location
Supplier Location
- China (Mainland)(20)
- India(2)
- United Kingdom(2)
- United States(2)
Business Type
Business Type
- Lab/Research institutions(3)
- Manufacturers(2)
- Other(1)
- Trading Company(12)
Certificates
Certificates
- ISO(3)
- Production License(2)
Exhibitions
Exhibitions
- CPhI China

Please post your buying leads>>

Display：

Manufacturer
Enterprise Authentication
Suppiers of more reward points first
New supplier

Please post your buying leads,so that our qualified suppliers will soon contact you!
*Required Fields

Reference

Transfer allyl esters to thioesters in solid phase condition: synthesis of peptide thioesters by Fmoc chemistry: All Rights Reserved. Transfer allyl esters to thioesters in solid phase condition: synthesis of peptide thioesters by Fmoc chemistry. Li, Lei; Wang, Pu (School of Pharmaceutical Science, Shandong University, Jinan 250012, Peop. Rep. China). Tetrahedron Letters, Volume Date 2007, 48(1), 29-32 (English) 2006 Elsevier Ltd. CODEN: TELEAY.Several substances like 73731-37-0 may be metioned in this study. ISSN: 0040-4039. DOCUMENT TYPE: Journal CA Section: 34 (Amino Acids, Peptides, and Proteins) A method to transfer allyl esters to thioesters under a solid phase condition has been developed to synthesize peptide thioesters. A Fmoc (Fmoc = 9-fluorenylmethyloxycarbonyl) chem. has been applied to synthesize the peptide allyl esters, which are selectively transferred to the expected peptide thioesters under solid phase synthesis conditions successfully. .

Inhibition of human b-tryptase by Bowman-Birk inhibitor derived peptides: creation of a new tri-functional inhibitor: Inhibition of human b-tryptase by Bowman-Birk inhibitor derived peptides: creation of a new tri-functional inhibitor. Scarpi, Dina; McBride, Jeffrey D.; Leatherbarrow, Robin J. ( Department of Chemistry, Imperial College London, London SW7 2AZ, UK). Bioorganic & Medicinal Chemistry, 12(23), 6045-6052 (English) 2004 Elsevier Ltd. CODEN: BMECEP. ISSN: 0968-0896. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Bowman-Birk inhibitor proteins (BBIs), which are potent inhibitors of chymotrypsin-like proteases, do not inhibit human b-tryptase despite this protein having a chymotrypsin-like fold. We have reported previously that, in contrast, BBI-derived peptides (whose sequences incorporate the solvent exposed reactive site loop motif) are able to inhibit human b-tryptase. This is due to their small size, which allows them to access the restricted active site(s) of tryptase, which has an unusual tetrameric arrangement with four active sites flanking a central pore. In this paper, we have examd. the possibility of creating addnl. interactions within this pore by adding extensions to the BBI-peptide motif. We have taken the core disulfide-bridged sequence SCTKSIPPQCY and examd. a series of extensions, at both the C- and N-termini, that bear a second pos. charged Lys residue at their end. The aim was to construct inhibitors that could make addnl. interactions in tryptase by spanning the gap between adjacent active sites in the enzyme, producing a double-headed inhibitor; a pos. charged group was used as the dominant specificity of this enzyme is for a pos. charged P1 residue. Both N- and C-terminal extensions are found to produce inhibitors of much increased potency, with a strong dependence of potency on chain length. Moreover, it was found that the C- and N-terminal extensions were able to synergize, with their combination on the same peptide producing an even better inhibitor with a potency 104-fold greater than the original sequence. We suggest that the C- and N-terminal extensions are picking up interactions with sep. addnl. sites on the tryptase, making the doubly extended BBI peptide a tri-functional tryptase inhibitor.Except for chemicals metioned above, 73731-37-0 and 116821-47-7 are also used. .

Detail of "73731-37-0"

L-Threonine,N-[(9H-fluoren-9-ylmethoxy)carbonyl]-

Famous Chemical Enterprises

Related products

Other Products

Supplier Location

Business Type

Certificates

Exhibitions

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

CAS No.73731-37-0 Fmoc-L-threonine

Reference