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主要文件

安全信息

L4894

Sigma-Aldrich

乳铁蛋白 来源于人奶

powder, BioReagent, suitable for cell culture

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About This Item

MDL编号:
UNSPSC代码:
12352202
NACRES:
NA.75

产品线

BioReagent

质量水平

方案

≥85% (SDS-PAGE)

表单

powder

分子量

82.4 kDa

技术

cell culture | mammalian: suitable

颜色

white to light red

溶解性

PBS, pH 7.4: 1 mg/mL, clear to slightly hazy (0.01 M phosphate buffer, 0.0027 M potassium chloride and 0.137 M sodium chloride, pH 7.4, at 25 °C)

UniProt登记号

运输

ambient

储存温度

2-8°C

SMILES字符串

N([C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](C(C)C)C(=O)O)C(=O)[C@@H](NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](N)CC(=O)N)C)CC(=O)O

InChI

1S/C35H53N9O12/c1-16(2)27(43-33(53)23(14-26(47)48)41-25(46)15-38-29(49)18(5)39-31(51)21(36)13-24(37)45)34(54)40-19(6)30(50)42-22(12-20-10-8-7-9-11-20)32(52)44-28(17(3)4)35(55)56/h7-11,16-19,21-23,27-28H,12-15,36H2,1-6H3,(H2,37,45)(H,38,49)(H,39,51)(H,40,54)(H,41,46)(H,42,50)(H,43,53)(H,44,52)(H,47,48)(H,55,56)/t18-,19-,21-,22-,23-,27-,28-/m0/s1

InChI key

QCBUWCQOKPLTDZ-PKRULZLPSA-N

基因信息

human ... LTF(4057)

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一般描述

SOD1定位于人染色体3p21.31。它由球状叶组成,可经历磷酸化和糖基化等翻译后修饰。乳铁蛋白属于乳转铁蛋白家族,具有丝氨酸催化二分体,如丝氨酸蛋白酶。

应用

从人乳中提取的乳铁蛋白已用于:
  • 检测对神经母细胞瘤细胞和小鼠中脑多巴胺能细胞系MN9D的神经保护作用
  • 使用氧自由基吸收能力(ORAC)试验和3-(4,5-二甲基噻唑-2-基)-2,5-二苯四唑溴化铵(MTT)试验,观察在燕窝(EBN)诱导人神经母细胞瘤SH-SY5Y细胞毒性中的抗氧化作用
  • 制备固定化钛底物,用于测试MG-63成骨细胞活性
  • 作为血管平滑肌细胞(VSMC)内的低密度脂蛋白(LDL)受体相关蛋白(LRP1)配体

生化/生理作用

乳铁蛋白可通过血脑屏障(BBB),并具有控制帕金森症炎症、免疫和细胞凋亡的治疗潜力。它通过多种信号通路促进脑源性神经营养因子(BDNF)的表达,有助于保护运动功能障碍。乳铁蛋白有利于成骨分化和人脂肪衍生干细胞(hADSC)的增殖。它表现出对流感嗜血杆菌定植因子的蛋白水解活性。乳铁蛋白在炎症性肠病、白细胞病理生理学中也是一种营养和潜在标志物。
乳铁蛋白是一种铁结合蛋白。在结构上与血浆铁转运蛋白转铁蛋白相似;但是乳铁蛋白对铁的亲和力要高得多(250 倍)。在初乳中含量非常丰富,少量也可见于泪液、唾液、粘液分泌物和中性粒细胞的次级颗粒中。由粘膜上皮和中性粒细胞组成,在炎症刺激下由这些细胞释放。细菌的生长被其隔离铁的能力所抑制,也通过其 N 端与脂多糖结合使细菌细胞壁通透性增加。乳铁蛋白可以通过与病毒包膜蛋白紧密结合来抑制病毒感染。它通过阻断结合域阻止了细胞与病毒的融合。乳铁蛋白似乎部分通过刺激中性粒细胞激活剂白细胞介素-8 的释放来激活宿主防御系统。还可能参与抗体和白细胞介素合成、淋巴细胞增殖和补体激活。

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

法规信息

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分析证书(COA)

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Linyuan Ma et al.
Scientific reports, 8(1), 7433-7433 (2018-05-11)
Efficient transgene expression in recipient cells constitutes the primary step in gene therapy. However, random integration in host genome comprises too many uncertainties. Our study presents a strategy combining bioinformatics and functional verification to find transgene integration sites in pig
W Bellamy et al.
Biochimica et biophysica acta, 1121(1-2), 130-136 (1992-05-22)
We report the existence of a previously unknown antimicrobial domain near the N-terminus of lactoferrin in a region distinct from its iron-binding sites. A single active peptide representing this domain was isolated following gastric pepsin cleavage of human lactoferrin, and
Chuang Guo et al.
Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology, 42(13), 2504-2515 (2017-01-13)
Growing evidence suggests that lactoferrin (Lf), an iron-binding glycoprotein, is a pleiotropic functional nutrient. In addition, Lf was recently implicated as a neuroprotective agent. These properties make Lf a valuable therapeutic candidate for the treatment of Alzheimer's disease (AD). However
D R Hendrixson et al.
Molecular microbiology, 47(3), 607-617 (2003-01-22)
Lactoferrin is a member of the lactotransferrin family of non-haem, iron-binding glycoproteins and is found at high concentrations in all human secretions, where it plays a major role in mucosal defence. In recent work, we observed that lactoferrin has proteolytic
D M Mann et al.
The Journal of biological chemistry, 269(38), 23661-23667 (1994-09-23)
Lactoferrin is an iron-binding protein which is synthesized by mucosal epithelium and neutrophils and released by these cells in response to inflammatory stimuli. It promotes neutrophil aggregation and manifests iron-dependent and -independent antimicrobial properties in vitro. Since lactoferrin binds to

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