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C1796

Sigma-Aldrich

Cecropin B

≥97% (HPLC), powder

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About This Item

Formule empirique (notation de Hill):
C176H301N51O42S
Numéro CAS:
Poids moléculaire :
3835.65
Numéro MDL:
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

225,00 €


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Niveau de qualité

Essai

≥97% (HPLC)

Forme

powder

Spectre d'activité de l'antibiotique

fungi

Mode d’action

cell membrane | interferes

Température de stockage

−20°C

Chaîne SMILES 

S(CC[C@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)Cc3c4c([nH]c3)cccc4)CCCCN)C(C)C)Cc2ccccc2)CCCCN)CCCCN)[C@H](CC)C)CCC(=O)O)CCCCN)C(=O)NCC(=O)N[C@@H](CCCN\C(

InChI

1S/C176H302N52O41S/c1-25-97(15)140(174(269)224-139(96(13)14)168(263)212-113(57-36-43-72-179)155(250)199-101(19)145(240)198-91-134(234)228-79-50-64-128(228)167(262)202-104(22)149(244)225-141(98(16)26-2)171(266)203-105(23)148(243)222-137(94(9)10)169(264)219-123(82-93(7)8)152(247)196-89-132(232)205-119(65-67-135(235)236)156(251)201-102(20)146(241)206-112(56-35-42-71-178)154(249)200-103(21)147(242)215-122(144(187)239)81-92(5)6)221-133(233)90-197-153(248)126(85-129(185)229)217-160(255)118(63-49-78-193-176(190)191)213-172(267)143(100(18)28-4)227-166(261)127(86-130(186)230)218-157(252)111(62-48-77-192-175(188)189)204-131(231)88-195-151(246)121(69-80-270-24)211-159(254)114(58-37-44-73-180)207-161(256)120(66-68-136(237)238)214-173(268)142(99(17)27-3)226-163(258)117(61-40-47-76-183)208-158(253)115(59-38-45-74-181)209-164(259)124(83-106-51-30-29-31-52-106)220-170(265)138(95(11)12)223-162(257)116(60-39-46-75-182)210-165(260)125(216-150(245)109(184)54-34-41-70-177)84-107-87-194-110-55-33-32-53-108(107)110/h29-33,51-53,55,87,92-105,109,111-128,137-143,194H,25-28,34-50,54,56-86,88-91,177-184H2,1-24H3,(H2,185,229)(H2,186,230)(H2,187,239)(H,195,246)(H,196,247)(H,197,248)(H,198,240)(H,199,250)(H,200,249)(H,201,251)(H,202,262)(H,203,266)(H,204,231)(H,205,232)(H,206,241)(H,207,256)(H,208,253)(H,209,259)(H,210,260)(H,211,254)(H,212,263)(H,213,267)(H,214,268)(H,215,242)(H,216,245)(H,217,255)(H,218,252)(H,219,264)(H,220,265)(H,221,233)(H,222,243)(H,223,257)(H,224,269)(H,225,244)(H,226,258)(H,227,261)(H,235,236)(H,237,238)(H4,188,189,192)(H4,190,191,193)/t97-,98-,99-,100-,101-,102-,103-,104-,105-,109-,111-,112-,113-,114-,115-,116-,117-,118-,119-,120-,121-,122-,123-,124-,125-,126-,127-,128-,137-,138-,139-,140-,141-,142-,143-/m0/s1

Clé InChI

YIQHNFUJWYYSEC-MQAAYMCRSA-N

Amino Acid Sequence

Lys-Trp-Lys-Val-Phe-Lys-Lys-Ile-Glu-Lys-Met-Gly-Arg-Asn-Ile-Arg-Asn-Gly-Ile-Val-Lys-Ala-Gly-Pro-Ala-Ile-Ala-Val-Leu-Gly-Glu-Ala-Lys-Ala-Leu-NH2

Description générale

Cecropin B is an antimicrobial peptide present in the hemolymph of the silk moth, Hyalophora cecropia. It is a member of the Cecropin class and possesses an α-helix-like structure.[1] 
Chemical structure: peptide

Application

Cecropin B has been used as an antibiotic peptide to study its cytotoxic potential in breast adenocarcinoma and mesothelioma cell lines.[1] It has also been used as an antimicrobial peptide to test the susceptibility of the Photorhabdus variants in minimal inhibitory concentration (MIC) assays.[2]

Actions biochimiques/physiologiques

Antibacterial peptide
Antibacterial peptide originally identified in moths (Hyalophora cecropia) and later in pig intestine.
Cecropin B is known for its antimicrobial activity. It displays antitumor effects in hepatocellular carcinoma, lymphoma, and leukemia cell lines.[1]

Autres remarques

Lyophilized from 0.1% TFA in H2O

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Les clients ont également consulté

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Chao-chao Luo et al.
Animal biotechnology, 24(1), 66-78 (2013-02-12)
The antibacterial peptide Cecropin B (CB), isolated from the giant silk moth, has been shown to effectively eliminate bacteria. In this study, the effects of transgenic CB on dairy goat mammary epithelial cells (DGMECs) and dairy goat mammary gland were
Yu-qing Hao et al.
Chinese medical journal, 118(2), 155-160 (2005-01-26)
Cecropin-XJ belongs to cecropin-B, which is the most potent antibacterial peptide found naturally. The aim of this study was to investigate the effects of cecropin-XJ on growth and adherence of oral cariogenic bacteria. Four oral cariogenic bacteria (Streptococcus mutans, Lactobacillus
P Peter Chiou et al.
Developmental and comparative immunology, 30(9), 797-806 (2005-12-15)
There are increasing evidence of the potential role of antimicrobial peptides in the regulation of immune responses in mammalian species. However, the effects of these peptides in fish have yet to be investigated. In this study, we examined the transcriptional
Zhongyuan Liu et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 66(Pt 7), 851-853 (2010-07-08)
Cecropin B is a 37-residue cationic antimicrobial peptide derived from the haemolymph of Bombyx mori. The precise mechanism by which cecropins exert their antimicrobial and cytolytic activities is not well understood. Crystals of cecropin B were obtained by the hanging-drop
Henrik Suttmann et al.
BMC urology, 8, 5-5 (2008-03-05)
This study evaluated the cytotoxic and antiproliferative efficacy of two well-characterized members of the Cecropin-family of antimicrobial peptides against bladder tumor cells and benign fibroblasts. The antiproliferative and cytotoxic potential of the Cecropins A and B was quantified by colorimetric

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