Transferrin is a monomeric serum glycoprotein (∼80,000 daltons) that binds to a specific receptor on the surface of vertebrate cells and delivers up to two Fe3+ atoms via receptor-mediated endocytosis—our labeled LDL complexes are useful tools for studying this phenomenon. Once iron-carrying transferrin proteins are inside endosomes, the acidic environment favors dissociation of iron from the transferrin–receptor complex. Following the release of iron, the apotransferrin is recycled to the plasma membrane, where it is released from its receptor to scavenge more iron. Fluorescent transferrin conjugates can therefore be used with fluorescent LDL to distinguish the lysosomally directed and recycling endosomal pathways.
These experiments are typically performed by adding fluorescently labeled transferrin to cultured cells and analyzing them by microscopy. We offer a biotinylated transferrin conjugate and more than 10 fluorescent versions.
Key Applications of Labeled Transferrin Some of the many applications for labeled transferrin include: • Image transferrin receptor dynamics using FRET • Observe receptor trafficking in live cells by confocal laser-scanning microscopy • Investigate events occurring during endosomal acidification • Measure transferrin receptor binding affinity in mammals and parasites
For Research Use Only. Not intended for any animal or human therapeutic or diagnostic use.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Detection MethodFluorescence
Dye TypeAlexa Fluor Dyes
Excitation/Emission556/573
FormSolid
Protein FamilyTransferrin
Quantity5 mg
Shipping ConditionRoom Temperature
Product LineAlexa Fluor
Product TypeTransferrin
pH7.2
Unit Size5 mg
Contents & Storage
Store in freezer (-5 to -30°C) and protect from light.
Citations & References (26)
Citations & References
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