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Rabbit Recombinant Monoclonal Lactoferrin antibody - conjugated to PE.

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Key facts

Isotype
IgG
Host species
Rabbit
Conjugation
PE
Excitation/Emission
Ex: 480;565nm, Em: 578nm
Storage buffer

pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: 98% PBS, 1% BSA

Form
Liquid
Clonality
Monoclonal

Immunogen

  • The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

Application
Target Binding Affinity
Reactivity
Expected
Dilution info
-
Notes

-

Application
Antibody Labelling
Reactivity
Expected
Dilution info
-
Notes

-

Target data

Function

Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Lactotransferrin. Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions (PubMed:11179314, PubMed:12693969, PubMed:14573629, PubMed:1599934, PubMed:3169987, PubMed:6802759). Has antimicrobial activity, which depends on the extracellular cation concentration (PubMed:6802759). Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane (PubMed:11179314, PubMed:12693969, PubMed:14573629, PubMed:1599934, PubMed:3169987, PubMed:6802759). Can also prevent bacterial biofilm development in P.aeruginosa infection (PubMed:12037568). Has weak antifungal activity against C.albicans (PubMed:11083624). Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth (PubMed:15166119). Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection (PubMed:17079302). Can inhibit papillomavirus infections (PubMed:17481742). Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling (PubMed:20345905). Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells (PubMed:19033648). Stimulates VEGFA-mediated endothelial cell migration and proliferation (PubMed:16842782). Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs) (PubMed:9359845). Also binds specifically to pneumococcal surface protein A (PspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA (PubMed:9359845). Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection (PubMed:17481742). N-terminal region shows strong antifungal activity against C.albicans (PubMed:11083624). Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site. Kaliocin-1. Has antimicrobial activity and is able to permeabilize different ions through liposomal membranes. Lactoferroxin-A. Has opioid antagonist activity (PubMed:1369293). Shows preference for mu-receptor (PubMed:1369293). Lactoferroxin-B. Has opioid antagonist activity (PubMed:1369293). Shows higher degrees of preference for kappa-receptors than for mu-receptors (PubMed:1369293). Lactoferroxin-C. Has opioid antagonist activity (PubMed:1369293). Shows higher degrees of preference for kappa-receptors than for mu-receptors (PubMed:1369293). The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions (PubMed:12535064). This function contributes to the antimicrobial activity (PubMed:12535064). Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites (PubMed:12535064). Isoform DeltaLf. Transcription factor with antiproliferative properties and ability to induce cell cycle arrest (PubMed:15222485). Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELENOH promoters (PubMed:22320386).

Alternative names

Recommended products

Rabbit Recombinant Monoclonal Lactoferrin antibody - conjugated to PE.

Key facts

Isotype
IgG
Conjugation
PE
Excitation/Emission
Ex: 480;565nm, Em: 578nm
Form
Liquid
Clonality
Monoclonal
Immunogen
  • The exact immunogen used to generate this antibody is proprietary information.
Clone number
EPR4337
Purification technique
Affinity purification Protein A
Concentration
Loading...

Storage

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle, Store in the dark

Notes

Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

This conjugated primary antibody is released using a quantitative quality control method that evaluates binding affinity post-conjugation and efficiency of antibody labeling.
For suitable applications and species reactivity, please refer to the unconjugated version of this clone. This conjugated antibody is eligible for the Abcam trial program.

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.
Activity summary

Lactoferrin also known as lactotransferrin is an iron-binding glycoprotein with a molecular weight of about 80 kDa. It predominantly exists in mammalian milk particularly in high concentrations in colostrum and is also found in various epithelial secretions such as saliva tears and nasal fluids. The liver and neutrophils also produce lactoferrin and it plays a significant role in the body's primary defense system. As an antibacterial agent lactoferrin sequesters free iron to limit bacterial growth and disrupt biofilms assisting in the protection against microbial invasions.

Biological function summary

Lactoferrin exhibits multiple functions beyond its antimicrobial properties. It contributes to immunomodulation by binding to specific receptors on immune cells enhancing phagocytosis and influencing cytokine production. Also it possesses anti-inflammatory and antioxidant properties. Lactoferrin interacts with cellular components including glycosaminoglycans and lipoproteins impacting the activity and expression of proteins within signaling and metabolic pathways. This multifaceted role places it as a critical participant in both innate and adaptive immune responses although it does not form part of a stable protein complex.

Pathways

Lactoferrin plays a significant role in the iron metabolism and immune response pathways. It tightly interacts with the transferrin receptor modulating iron uptake and distribution across tissues which helps prevent iron overload and oxidative stress. Furthermore lactoferrin links with the toll-like receptor pathways particularly TLR4 which enables the modulation of innate immune responses against pathogens. By influencing nuclear factor kappa B (NF-kB) signaling lactoferrin impacts inflammation and immune responses working together with proteins such as ferritin and hepcidin.

Associated diseases and disorders

Lactoferrin has relevancy to diseases like anemia of chronic disease and inflammatory bowel disease (IBD). Its role in regulating iron homeostasis makes it essential for preventing anemia associated with chronic inflammation. Lactoferrin mitigates dysregulated immune responses in IBD potentially reducing inflammation and promoting gut health. Disease-modifying properties of lactoferrin connect it to glycoproteins like transferrin and inflammatory mediators demonstrating its potential therapeutic importance.

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