来自人血清的转铁蛋白,Alexa Fluor™ 568 偶联物
来自人血清的转铁蛋白,Alexa Fluor™ 568 偶联物
Invitrogen™

来自人血清的转铁蛋白,Alexa Fluor™ 568 偶联物

转铁蛋白是一种单体血清糖蛋白(∼80,000 道尔顿),其通过受体介导的内吞作用结合到脊椎动物细胞表面的特定受体上,并递送多达 2 个 Fe3+ 原子 — 标记的了解更多信息
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货号数量
T233655 mg
货号 T23365
价格(CNY)
6,808.00
飞享价
Ends: 31-Dec-2025
8,988.00
共减 2,180.00 (24%)
5 mg
添加至购物车
数量:
5 mg
价格(CNY)
6,808.00
飞享价
Ends: 31-Dec-2025
8,988.00
共减 2,180.00 (24%)
5 mg
添加至购物车
转铁蛋白是一种单体血清糖蛋白(∼80,000 道尔顿),其通过受体介导的内吞作用结合到脊椎动物细胞表面的特定受体上,并递送多达 2 个 Fe3+ 原子 — 标记的 LDL 复合物是研究该现象的有用工具。携带铁的转铁蛋白进入核内体后,酸性环境即可促使铁离子从转铁蛋白–受体复合物中解离。铁释放后,脱铁转铁蛋白被回收至细胞膜中,其从受体中释放出来以结合更多的铁。因此,荧光转铁蛋白偶联物可以与荧光 LDL 配合使用,以区分溶菌体定向途径和内涵体回收通路。

这些实验通常是通过向培养细胞中加入荧光标记的转铁蛋白并通过显微镜进行分析。我们提供生物素化的转铁蛋白偶联物及超过 10 种荧光形式。

转铁蛋白规格:

标记 (Ex/Em):Alexa Fluor™ 568 (578/603)

含量:15 mg 固体(含 5 mg 转铁蛋白偶联物)

标记的转铁蛋白的主要应用
标记的转铁蛋白的其中一些应用包括:
•使用 FRET 对转铁蛋白受体动力学进行成像
• 通过共聚焦激光扫描显微镜检查观察活细胞中的受体转运
• 研究内涵体酸化期间发生的事件
• 测量哺乳动物和寄生虫中的转铁蛋白受体结合亲和力

仅供研究使用。不得用于任何动物或人类的治疗或诊断。
仅供科研使用。不可用于诊断程序。
规格
检测方法荧光
染料类型Alexa Fluor 染料
激发/发射578/603
形式实心
蛋白质家族转铁蛋白
数量5 mg
运输条件室温
产品线Alexa Fluor
产品类型转铁蛋白
pH7.2
Unit Size5 mg
内容与储存
储存在冰箱(-5 至 -30°C)中并避光。

常见问题解答 (FAQ)

Is Transferrin From Human Serum, Alexa Fluor 568 Conjugate (Cat. No. T23365) holotransferrin (saturated with iron)? How is the fluorophore conjugated to it?

Transferrin From Human Serum, Alexa Fluor 568 Conjugate is holotransferrin (saturated with iron). Lysine residues of transferrin are used for conjugation of the fluorophore. On the Certificate of Analysis, you can find information regarding the degree of labeling (number of fluorophores per one protein molecule).

Find additional tips, troubleshooting help, and resources within our Cell Analysis Support Center.

引用和文献 (22)

引用和文献
Abstract
Inactivation of NPC1L1 causes multiple lipid transport defects and protects against diet-induced hypercholesterolemia.
Authors:Davies JP, Scott C, Oishi K, Liapis A, Ioannou YA
Journal:J Biol Chem
PubMed ID:15671032
'NPC1L1, a recently identified relative of Niemann-Pick C1, was characterized to determine its subcellular location and potential function(s). NPC1L1 was highly expressed in HepG2 cells and localized in a subcellular vesicular compartment rich in the small GTPase Rab5. mRNA expression profiling revealed significant differences between mouse and man with highest ... More
Dynamics and function of phospholipase D and phosphatidic acid during phagocytosis.
Authors:Corrotte M, Chasserot-Golaz S, Huang P, Du G, Ktistakis NT, Frohman MA, Vitale N, Bader MF, Grant NJ
Journal:Traffic
PubMed ID:16497229
'Phospholipase D (PLD) produces phosphatidic acid (PA), an established intracellular signalling lipid that has been also implicated in vesicular trafficking, and as such, PLD could play multiple roles during phagocytosis. Using an RNA interference strategy, we show that endogenous PLD1 and PLD2 are necessary for efficient phagocytosis in murine macrophages, ... More
Rab11-family interacting proteins define spatially and temporally distinct regions within the dynamic Rab11a-dependent recycling system.
Authors:Baetz NW, Goldenring JR,
Journal:Mol Biol Cell
PubMed ID:23283983
'The Rab11-family interacting proteins (Rab11-FIPs) facilitate Rab11-dependent vesicle recycling. We hypothesized that Rab11-FIPs define discrete subdomains and carry out temporally distinct roles within the recycling system. We used live-cell deconvolution microscopy of HeLa cells expressing chimeric fluorescent Rab11-FIPs to examine Rab11-FIP localization, transferrin passage through Rab11-FIP-containing compartments, and overlap among ... More
Site-specific protein labeling by Sfp phosphopantetheinyl transferase.
Authors:Yin J, Lin AJ, Golan DE, Walsh CT,
Journal:Nat Protoc
PubMed ID:17406245
'Sfp phosphopantetheinyl transferase covalently attaches small-molecule probes including biotin and various organic fluorophores to a specific serine residue in the peptidyl carrier protein (PCP) or a short 11-residue peptide tag ybbR through a phosphopantetheinyl linker. We describe here a protocol for site-specific protein labeling by Sfp-catalyzed protein post-translational modification that ... More
Correlative light-electron microscopy (CLEM) combining live-cell imaging and immunolabeling of ultrathin cryosections.
Authors:van Rijnsoever C, Oorschot V, Klumperman J,
Journal:Nat Methods
PubMed ID:18974735
'The visualization of fluorescent proteins in living cells is a powerful approach to study intracellular dynamics. A limitation of fluorescence imaging, however, is that it lacks fine structural information; a fluorescent spot could represent an entire organelle, an organellar subdomain or even aggregates of proteins or membranes. These limitations can ... More