方案
≥98% (HPLC)
表单
powder
颜色
yellow to brown
mp
108-110 °C (lit.)
储存温度
2-8°C
SMILES字符串
BrCC(=O)c1ccc(Br)cc1
InChI
1S/C8H6Br2O/c9-5-8(11)6-1-3-7(10)4-2-6/h1-4H,5H2
InChI key
FKJSFKCZZIXQIP-UHFFFAOYSA-N
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Youngjin Park et al.
Archives of insect biochemistry and physiology, 60(3), 105-115 (2005-10-20)
We report on a secretory phospholipase A2 (sPLA2) associated with membrane-enriched fractions prepared from hemocytes of the tobacco hornworms, Manduca sexta. Virtually no PLA2 activity was detected in serum of immunologically naive or bacterially challenged hornworms. PLA2 activity was detected
Daniela P Marchi-Salvador et al.
Biochimica et biophysica acta, 1794(11), 1583-1590 (2009-07-21)
For the first time, the structure of a catalytic inactive phospholipase A(2) homolog (Lys49-PLA(2)s) complexed with p-bromophenacyl bromide (BPB) has been solved by X-ray crystallography. Lys49-PLA(2)s are among the main components of Viperidae snake venoms, causing myonecrosis and other actions
Rodrigo G Stábeli et al.
Comparative biochemistry and physiology. Toxicology & pharmacology : CBP, 142(3-4), 371-381 (2006-01-31)
MjTX-II, a myotoxic phospholipase A(2) (PLA(2)) homologue from Bothrops moojeni venom, was functionally and structurally characterized. The MjTX-II characterization included: (i) functional characterization (antitumoral, antimicrobial and antiparasitic effects); (ii) effects of structural modifications by 4-bromophenacyl bromide (BPB), cyanogen bromide (CNBr)
Angelo J Magro et al.
Acta crystallographica. Section D, Biological crystallography, 61(Pt 12), 1670-1677 (2005-11-23)
The crystal structure of an acidic phospholipase A(2) isolated from Bothrops jararacussu venom (BthA-I) chemically modified with p-bromophenacyl bromide (BPB) has been determined at 1.85 Angstroms resolution. The catalytic, platelet-aggregation inhibition, anticoagulant and hypotensive activities of BthA-I are abolished by
P S F Barbosa et al.
Toxicon : official journal of the International Society on Toxinology, 46(4), 376-386 (2005-08-24)
Bothrops jararacussu myotoxin I (BthTx-I; Lys 49) and II (BthTX-II; Asp 49) were purified by ion-exchange chromatography and reverse phase HPLC. In this work we used the isolated perfused rat kidney method to evaluate the renal effects of B. jararacussu
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