Native Human Lactoferrin protein (ab90354)
Key features and details
- Expression system: Native
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
Description
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Product name
Native Human Lactoferrin protein
See all Lactoferrin proteins and peptides -
Purity
> 95 % SDS-PAGE. -
Expression system
Native -
Protein length
Full length protein -
Animal free
No -
Nature
Native -
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Species
Human
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab90354 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
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Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.
pH: 8.00
Constituents: 1.58% Tris HCl, 1.74% Sodium chloride
General Info
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Alternative names
- GIG12
- Growth inhibiting protein 12
- HLF2
see all -
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 has antimicrobial activity which depends on the extracellular cation concentration.
Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.
The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. -
Sequence similarities
Belongs to the transferrin family.
Contains 2 transferrin-like domains. -
Cellular localization
Secreted. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab90354 has not yet been referenced specifically in any publications.