来自人血清的转铁蛋白,Alexa Fluor™ 546 偶联物
来自人血清的转铁蛋白,Alexa Fluor™ 546 偶联物
Invitrogen™

来自人血清的转铁蛋白,Alexa Fluor™ 546 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
T233645 mg
货号 T23364
价格(CNY)
8,399.00
5 mg
添加至购物车
数量:
5 mg
价格(CNY)
8,399.00
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™ 546 (556/573)

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556/573
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。

引用和文献 (26)

引用和文献
Abstract
Grp1-associated scaffold protein (GRASP) is a regulator of the ADP ribosylation factor 6 (Arf6)-dependent membrane trafficking pathway.
Authors:Venkataraman A, Nevrivy DJ, Filtz TM, Leid M,
Journal:Cell Biol Int
PubMed ID:22931251
GRASP interacts with Grp1 (general receptor for phosphoinositides 1; cytohesin 3), which catalyses nucleotide exchange on and activation of Arf6 (ADP-ribosylation factor-6). Arf6 is a low-molecular-mass GTPase that regulates key aspects of endocytic recycling pathways. Overexpressed GRASP accumulated in the juxtanuclear ERC (endocytic recycling compartment). GRASP co-localized with a constitutively ... More
Amino acid residues critical for endoplasmic reticulum export and trafficking of platelet-activating factor receptor.
Authors:Hirota N, Yasuda D, Hashidate T, Yamamoto T, Yamaguchi S, Nagamune T, Nagase T, Shimizu T, Nakamura M,
Journal:J Biol Chem
PubMed ID:20007715
'Several residues are conserved in the transmembrane domains (TMs) of G-protein coupled receptors. Here we demonstrate that a conserved proline, Pro(247), in TM6 of platelet-activating factor receptor (PAFR) is required for endoplasmic reticulum (ER) export and trafficking after agonist-induced internalization. Alanine-substituted mutants of the conserved residues of PAFRs, including P247A, ... More
TLR9 signals after translocating from the ER to CpG DNA in the lysosome.
Authors:Latz E, Schoenemeyer A, Visintin A, Fitzgerald KA, Monks BG, Knetter CF, Lien E, Nilsen NJ, Espevik T, Golenbock DT
Journal:Nat Immunol
PubMed ID:14716310
'Microbial DNA sequences containing unmethylated CpG dinucleotides activate Toll-like receptor 9 (TLR9). We have found that TLR9 is localized to the endoplasmic reticulum (ER) of dendritic cells (DCs) and macrophages. Because there is no precedent for immune receptor signaling in the ER, we investigated how TLR9 is activated. We show ... More
Regulation of endocytosis via the oxygen-sensing pathway.
Authors:Wang Y, Roche O, Yan MS, Finak G, Evans AJ, Metcalf JL, Hast BE, Hanna SC, Wondergem B, Furge KA, Irwin MS, Kim WY, Teh BT, Grinstein S, Park M, Marsden PA, Ohh M,
Journal:Nat Med
PubMed ID:19252501
'Tumor hypoxia is associated with disease progression, resistance to conventional cancer therapies and poor prognosis. Hypoxia, by largely unknown mechanisms, leads to deregulated accumulation of and signaling via receptor tyrosine kinases (RTKs) that are critical for driving oncogenesis. Here, we show that hypoxia or loss of von Hippel-Lindau protein--the principal ... More
Chemical-genetic inhibition of a sensitized mutant myosin Vb demonstrates a role in peripheral-pericentriolar membrane traffic.
Authors:Provance DW, Gourley CR, Silan CM, Cameron LC, Shokat KM, Goldenring JR, Shah K, Gillespie PG, Mercer JA
Journal:Proc Natl Acad Sci U S A
PubMed ID:14766983
'Selective, in situ inhibition of individual unconventional myosins is a powerful approach to determine their specific physiological functions. Here, we report the engineering of a myosin Vb mutant that still hydrolyzes ATP, yet is selectively sensitized to an N(6)-substituted ADP analog that inhibits its activity, causing it to remain tightly ... More