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140896-21-5

中文名稱 ILE-LEU-PRO-TRP-LYS-TRP-PRO-TRP-TRP-PRO-TRP-ARG-ARG-NH2
英文名稱 INDOLICIDIN
CAS 140896-21-5
分子式 C100H132N26O13
分子量 1906.28
MOL 文件 140896-21-5.mol
更新日期 2026/07/23 09:59:41
140896-21-5 結(jié)構式 140896-21-5 結(jié)構式

基本信息

中文別名
IR-13-NH2
INDOLICIDIN肽
英文別名
INDOLICIDIN
Indolicidin TFA
ILPWKWPWWPWRR-NH2
IndolicidinIndolicid
Indolicidin, ≥97% (HPLC)
42: PN: US7381704 SEQID: 42 claimed sequence
ILE-LEU-PRO-TRP-LYS-TRP-PRO-TRP-TRP-PRO-TRP-ARG-ARG-NH2
H-ILE-LEU-PRO-TRP-LYS-TRP-PRO-TRP-TRP-PRO-TRP-ARG-ARG-NH2
L-ArgininaMide,L-isoleucyl-L-leucyl-L-prolyl-L-tryptophyl-L-lysyl-L-tryptophyl-L-prolyl-L-tryptophyl-L-tryptophyl-L-prolyl-L-tryptophyl-L-arginyl-

物理化學性質(zhì)

密度1.45±0.1 g/cm3(Predicted)
RTECS號NM1890250
儲存條件−20°C
溶解度可微溶于水
酸度系數(shù)(pKa)13.29±0.46(Predicted)
形態(tài)粉末
顏色White to off-white
水溶解性Soluble in water (1 mg/ml).
序列H--Ile-Leu-Pro-Trp-Lys-Trp-Pro-Trp-Trp-Pro-Trp-Arg-Arg-NH2

應用領域

多肽
抗菌肽Indolicidin是從牛中性粒細胞胞質(zhì)顆粒中分離得到的一種抗菌肽。其結(jié)構為ILPWKWPWWPWRR ̄NH2,僅包含6種共13個氨基酸,是目前為止已知的最小的天然線性抗菌肽之一。該多肽的羧基端被酰胺化,共包含 39% 的色氨酸殘基和 23%的脯氨酸殘基。這是 Cathelicidins 家族甚至是目前已知蛋白質(zhì)中色氨酸含量最高的多肽之一。Indolicidin抗菌譜廣,對多種需氧革蘭氏陰性菌、革蘭氏陽性菌和真菌都有很強的抗菌活性。
參考質(zhì)量標準
外觀:白色粉末
純度(HPLC) ≥98.0%
醋酸根含量≤12.0%
水分含量≤8.0%
肽含量≥80.0%
內(nèi)毒素≤50EU/mg
氨基酸組成分析≤±10%

安全數(shù)據(jù)

WGK Germany3
抗菌肽Indolicidin價格(試劑級)
報價日期產(chǎn)品編號產(chǎn)品名稱CAS號包裝價格
2026/06/05HY-P0261ILE-LEU-PRO-TRP-LYS-TRP-PRO-TRP-TRP-PRO-TRP-ARG-ARG-NH2
Indolicidin
140896-21-51mg1120元
2026/06/05HY-P0261ILE-LEU-PRO-TRP-LYS-TRP-PRO-TRP-TRP-PRO-TRP-ARG-ARG-NH2
Indolicidin
140896-21-55mg2520元
2026/06/05HY-P0261抗菌肽Indolicidin
Indolicidin
140896-21-510 mg3780元

常見問題列表

生物活性
Indolicidin是從牛嗜中性粒細胞的細胞質(zhì)顆粒中純化的有效的抗微生物肽。
體外研究

Indolicidin is comprised of 13 amino acids, 5 of which are tryptophan residues, and the carboxylterminal arginine is carboxamidated. Indolicidin has the highest tryptophan content of any known protein. The multiple tryptophan residues may play an important role in the function of this unique antibiotic peptide. Indolicidin is a tridecapeptide amide which possesses in vitro bactericidal activities comparable with the most active of the defensin or bactenecin peptides. Indolicidin binds purified surface lipopolysaccharide with high affinity and permeabilized the outer membrane of Escherichia coli to the small hydrophobic molecule 1-N-phenylnapthylamine (Mr 200), results consistent with indolicidin crossing the outer membrane via the self-promoted uptake pathway. The methyl esterification of indolicidin's carboxyl terminus increases its activity for Gram-negative and Gram-positive bacteria. In Gram-negative bacteria this is associated with an increased binding to lipopolysaccharide and increased permeabilization of the outer membrane. The cytoplasmic membrane is the site of action of indolicidin as assayed in Escherichia coli by the unmasking of cytoplasmic beta-galactosidase due to membrane permeabilization.

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