LTF Human

Lactoferrin Human (Breast Milk)
Cat. No.
BT2087
Source
Human breast milk.
Synonyms
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

The Human Lactoferrin produced from Human breast milk has a molecular mass of 76.165kDa (calculated without glycosylation) containing 691 amino acid residues.

Product Specs

Introduction
Lactoferrin, a glycoprotein in the transferrin family, plays a crucial role in iron binding. Found in human breast milk and various secretions like tears, saliva, and bronchial fluids, it exhibits a high affinity for iron, binding two molecules. Its iron withholding mechanism inhibits bacterial growth, while the N-terminal region acts as an antimicrobial peptide. Synergistically, lactoferrin enhances the activity of lysozyme. This multifunctional protein, often recognized as an innate defense protein, provides a primary defense against pathogens. Its capabilities encompass iron binding, antibacterial, antifungal, and antiviral activities, antioxidant properties, and immunomodulatory functions. Lactoferrin's diverse beneficial attributes make it a promising candidate for various product applications. Ongoing research continues to unravel its diverse biological functions.
Description
Human Lactoferrin, derived from human breast milk, possesses a molecular weight of 76.165 kDa (excluding glycosylation). Its structure consists of 691 amino acid residues.
Physical Appearance
The product appears as a white, lyophilized (freeze-dried) powder after filtration.
Formulation
The LTF protein undergoes a 0.4µm filtration process followed by lyophilization. It is prepared in a solution containing 0.5 mg/ml of protein in a buffer of 0.05M phosphate and 0.075M NaCl, adjusted to a pH of 7.4.
Solubility
To create a working stock solution, add deionized water to achieve a concentration of approximately 0.5 mg/ml. Allow the lyophilized pellet to dissolve completely. Note: This product is not sterile. Prior to cell culture use, filter the solution through an appropriate sterile filter.
Stability
For long-term storage, keep the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize repeated freezing and thawing cycles. Reconstituted protein remains stable at 4°C for a limited time, showing no alterations for up to two weeks.
Purity
SDS-PAGE analysis indicates a purity exceeding 95.0%.
Synonyms
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
Source
Human breast milk.
Amino Acid Sequence
GRRRSVQWCA VSQPEATKCF QWQRNMRKVR GPPVSCIKRD SPIQCIQAIA ENRADAVTLD GGFIYEAGLA PYKLRPVAAE VYGTERQPRT HYYAVAVVKK GGSFQLNELQ GLKSCHTGLR RTAGWNVPIG TLRPFLNWTG PPEPIEAAVA RFFSASCVPG ADKGQFPNLC RLCAGTGENK CAFSSQEPYF SYSGAFKCLR DGAGDVAFIR ESTVFEDLSD EAERDEYELL CPDNTRKPVD KFKDCHLARV PSHAVVARSV NGKEDAIWNL LRQAQEKFGK DKSPKFQLFG SPSGQKDLLF KDSAIGFSRV PPRIDSGLYL GSGYFTAIQN LRKSEEEVAA RRARVVWCAV GEQELRKCNQ WSGLSEGSVT CSSASTTEDC IALVLKGEAD AMSLDGGYVY TAGKCGLVPV LAENYKSQQS SDPDPNCVDR PVEGYLAVAV VRRSDTSLTW NSVKGKKSCH TAVDRTAGWN IPMGLLFNQT GSCKFDEYFS QSCAPGSDPR SNLCALCIGD EQGENKCVPN SNERYYGYTG AFRCLAENAG DVAFVKDVTV LQNTDGNNNE AWAKDLKLAD FALLCLDGKR KPVTEARSCH LAMAPNHAVV SRMDKVERLK QVLLHQQAKF GRNGSDCPDK FCLFQSETKN LLFNDNTECL ARLHGKTTYE KYLGPQYVAG ITNLKKCSTS PLLEACEFLR K.

Product Science Overview

Discovery and Structure

Lactoferrin was first identified in bovine milk in 1939, but it wasn’t until the 1960s that its structure and functions were thoroughly studied. It is a globular glycoprotein with a molecular mass of approximately 80 kDa. Lactoferrin has the ability to bind iron, which is central to its biological functions .

Concentration in Breast Milk

Human colostrum, the first milk produced after childbirth, contains the highest concentration of lactoferrin, followed by mature breast milk. The concentration of lactoferrin in human milk is significantly higher than in cow’s milk, making it particularly beneficial for human infants .

Biological Functions

Lactoferrin serves multiple roles in the body, particularly in the immune system:

  1. Antimicrobial Activity: Lactoferrin has bactericidal, fungicidal, and antiviral properties. It binds to iron, making it unavailable to bacteria, which require iron for growth. This iron-binding property helps inhibit the growth of pathogenic bacteria .

  2. Anti-inflammatory Properties: Lactoferrin helps modulate the inflammatory response, reducing inflammation in the body. This is particularly important for infants, whose immune systems are still developing .

  3. Antioxidant Activity: Lactoferrin acts as an antioxidant, protecting cells from damage caused by free radicals. This contributes to the overall health and well-being of infants .

  4. Iron Absorption: Lactoferrin facilitates the absorption of iron in the intestine, ensuring that infants receive adequate iron for their growth and development .

  5. Immune System Support: Lactoferrin interacts with various components of the immune system, enhancing the body’s ability to fight infections. It is constantly produced and released into saliva, tears, and other secretions, providing a first line of defense against pathogens .

Clinical Applications and Research

Lactoferrin has been studied for its potential therapeutic applications. It is used as a supplement to boost the immune system and has been investigated for its role in preventing respiratory tract infections. Research is ongoing to explore its potential benefits in various health conditions, including its role in immunity with COVID-19 in mind .

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