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Apo Lactoferrin from Human Breast Milk Proteins Molecular Depot
Apo Lactoferrin from Human Breast Milk Proteins Molecular Depot
Apo Lactoferrin from Human Breast Milk Proteins Molecular Depot
Apo Lactoferrin from Human Breast Milk Proteins Molecular Depot

Apo Lactoferrin from Human Breast Milk

$595.00

    Catalog Number: B2012199 (5 mg)

    Apo Lactoferrin from Human Breast Milk is a 5 mg biotechnology-grade lyophilized iron-depleted glycoprotein used for iron-binding biology, host defense protein research, oxidative stress studies, and biochemical assay development. This apo-lactoferrin preparation is ideal for investigating iron sequestration, protein-mediated signaling, iron-loading state effects, and lactoferrin-dependent biological activity in biochemical, cell-based, and mechanistic research workflows. The lyophilized format supports flexible reconstitution for iron-sensitive protein studies and comparative apo versus holo lactoferrin experiments. Custom bulk amounts of this product are available upon request.

    Products are for in vitro research use only (RUO).

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Apo Lactoferrin from Human Breast Milk – Research Use Only

Apo Lactoferrin from Human Breast Milk is a biotechnology-grade iron-depleted glycoprotein supplied as a 5 mg lyophilized preparation for research applications involving iron-binding biology, host defense proteins, cell signaling, oxidative stress, and protein interaction studies. Apo-lactoferrin represents the iron-unsaturated form of lactoferrin, making it especially useful in workflows where researchers want to investigate iron sequestration, protein-mediated biological effects, and lactoferrin-dependent biochemical activity. This reagent is well suited for laboratories studying innate immunity, protein function, iron homeostasis, and related biochemical pathways.

Catalog number: B2012199
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 5 mg
Molecular Weight or Concentration: 78 kDa
Supplied as: Lyophilized
Applications: Iron-binding biology, host defense protein research, oxidative stress studies, cell signaling, and biochemical assay development
Storage: -20°C
Keywords: Apo-Lactoferrin, apolactoferrin, apo-lf
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um.

Scientific Overview

Lactoferrin is a multifunctional iron-binding glycoprotein found in a variety of biological secretions and tissues, where it is associated with iron regulation, protein-mediated host defense mechanisms, and diverse cellular interactions. The apo form of lactoferrin refers to the iron-unsaturated state, which is especially relevant in experimental systems focused on iron availability, protein-ligand interaction, and metal-dependent biological responses.

In research settings, apo-lactoferrin is frequently studied in relation to iron sequestration, oxidative balance, cellular signaling pathways, protein binding behavior, and biomolecular regulation. Because its biological properties may differ from holo-lactoferrin or iron-saturated forms, apo-lactoferrin is particularly useful for mechanistic experiments where the role of iron loading state is important to assay interpretation.

Applications

  • Iron-binding and iron homeostasis research
  • Studies of host defense proteins and protein-mediated biological interactions
  • Oxidative stress and redox-related biochemical workflows
  • Cell signaling and protein function studies
  • Comparative analysis of apo- versus holo-lactoferrin behavior

Usage & Handling Guidance

Store the lyophilized protein at -20°C as specified. Reconstitute in an appropriate buffer suited to the intended assay or biochemical workflow. For studies where iron loading state is experimentally important, researchers should use conditions that minimize unintended metal contamination and validate protein behavior within the intended system.

  • Recommended applications: Iron-binding studies, protein interaction assays, signaling research, and biochemical method development
  • Preparation: Reconstitute in suitable buffer and optimize concentration for the intended protocol
  • Handling: Use low-metal handling conditions where iron-sensitive workflows are important
  • Workflow note: Functional behavior should be validated in the end-user assay system

What You Get

  • 5 mg of Apo Lactoferrin from Human Breast Milk
  • Lyophilized protein reagent for research use
  • Biotechnology-grade preparation suitable for biochemical workflows
  • Useful for iron-related and protein function studies
  • For research use only (RUO)

Why Researchers Choose It

  • Useful for studying the iron-unsaturated form of lactoferrin
  • Relevant to iron homeostasis, host defense, and signaling workflows
  • Supports comparison between apo and holo protein states
  • Suitable for mechanistic biochemical and protein interaction studies
  • Lyophilized format supports flexible preparation and storage

Frequently Asked Questions (FAQ)

  • What does “apo-lactoferrin” mean?
    Apo-lactoferrin refers to the iron-unsaturated form of lactoferrin, meaning the protein is not fully loaded with iron.
  • Why is the apo form useful in research?
    It is especially useful in experiments involving iron sequestration, iron-dependent biological responses, and comparative studies of protein function under different iron-loading conditions.
  • What types of workflows is this product suited for?
    It is commonly used in iron-binding studies, oxidative stress research, protein interaction assays, signaling studies, and related biochemical workflows.
  • How should this product be handled after reconstitution?
    It should be prepared in an appropriate buffer and handled under conditions suitable for the intended assay, especially when metal-sensitive performance is important.
  • Can this product be used for clinical or therapeutic applications?
    No. This product is supplied strictly for research use only and is not intended for diagnostic or therapeutic use.
This product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use in humans or animals.

References

  • Reyes-López M, Ramírez-Rico G, Serrano-Luna J, de la Garza M. Activity of Apo-Lactoferrin on Pathogenic Protozoa. Pharmaceutics. 2022 Aug 15;14(8):1702. Reference
  • Zhang Z, Lu M, Chen C, Tong X, Li Y, Yang K, Lv H, Xu J, Qin L. Holo-lactoferrin: the link between ferroptosis and radiotherapy in triple-negative breast cancer. Theranostics. 2021 Jan 1;11(7):3167-3182. Reference
  • Ramírez-Rico G, Martinez-Castillo M, Avalos-Gómez C, de la Garza M. Bovine apo-lactoferrin affects the secretion of proteases in Mannheimia haemolytica A2. Access Microbiol. 2021 Oct 25;3(10):000269. Reference
  • Zakharova ET, Kostevich VA, Sokolov AV, Vasilyev VB. Human apo-lactoferrin as a physiological mimetic of hypoxia stabilizes hypoxia-inducible factor-1 alpha. Biometals. 2012 Dec;25(6):1247-59. Reference
  • Avalos-Gómez C, Reyes-López M, Ramírez-Rico G, Díaz-Aparicio E, Zenteno E, González-Ruiz C, de la Garza M. Effect of apo-lactoferrin on leukotoxin and outer membrane vesicles of Mannheimia haemolytica A2. Vet Res. 2020 Mar 5;51(1):36. Reference
  • Akilo OD, Kumar P, Choonara YE, Pradeep P, du Toit LC, Pillay V. Hypothesis: apo-lactoferrin-Galantamine Proteo-alkaloid Conjugate for Alzheimer’s disease Intervention. J Cell Mol Med. 2018 Mar;22(3):1957-1963. Reference
  • Luzi C, Brisdelli F, Iorio R, Bozzi A, Carnicelli V, Di Giulio A, Lizzi AR. Apoptotic effects of bovine apo-lactoferrin on HeLa tumor cells. Cell Biochem Funct. 2017 Jan;35(1):33-41. Reference
  • Mikulic N, Uyoga MA, Mwasi E, Stoffel NU, Zeder C, Karanja S, Zimmermann MB. Iron Absorption is Greater from Apo-Lactoferrin and is Similar Between Holo-Lactoferrin and Ferrous Sulfate: Stable Iron Isotope Studies in Kenyan Infants. J Nutr. 2020 Dec 10;150(12):3200-3207. Reference
  • Liu H, Wu H, Zhu N, Xu Z, Wang Y, Qu Y, Wang J. Lactoferrin protects against iron dysregulation, oxidative stress, and apoptosis in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced Parkinson’s disease in mice. J Neurochem. 2020 Feb;152(3):397-415. Reference
  • Conio M, Rajan E, Sorbi D, Norton I, Herman L, Filiberti R, Gostout CJ. Comparative performance in the porcine esophagus of different solutions used for submucosal injection. Gastrointest Endosc. 2002 Oct;56(4):513-6. Reference

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Copy of Technical Specifications

FeatureDetails
Viewing Head Siedentopf type trinocular head, inclined at 30°, Interpupillary adjustment 53mm to 75mm, graduated diopter on left eyetube (30mm I.D. eyetubes)
Eyepieces SWH10X Widefield high eyepoint eyepiece, Field No. 22, tube O.D. 30.0 mm
Nosepiece Quintuple
Quintuple LWD Planachromat Phase 10x, 20x
Condenser TC Condenser N.A. 0.30, W.D. 73.0mm
Stage180mm(X) x 245mm(Y) plain stage with replaceable glass insert with 45mm opening, Glass Stage plate insert
IlluminationKoehler without iris, with phase slider, 3W LED
WarrantyLIMITED LIFETIME WARRANTY

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