LTF Human S.Plasma
Lactoferrin Human (Seminal Plasma)
Cat. No.
BT2164
Source
Human seminal plasma.
Synonyms
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Purity greater than 90% 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 pooled Human seminal plasma has a molecular mass of 76.165kDa (calculated without glycosylation) containing 691 amino acid residues.
Product Specs
Introduction
Lactoferrin, a glycoprotein belonging to the transferrin family, plays a crucial role in iron binding. Found in human breast milk and various epithelial secretions such as tears, saliva, and bronchial fluid, lactoferrin exhibits a high affinity for binding two iron molecules. Its iron-withholding capability contributes to its antibacterial properties, while its N-terminal region functions as an antimicrobial peptide. Notably, lactoferrin synergistically interacts with lysozyme, enhancing the activity of both proteins. As a multifunctional protein, lactoferrin participates in various physiological processes, acting as a vital component of the innate immune system. Its diverse functions include iron binding, antibacterial, antifungal, and antiviral activities, antioxidant properties, and immunomodulatory effects, making it a promising candidate for various product applications. Extensive research is ongoing to elucidate the diverse biological functions of lactoferrin.
Description
Human Lactoferrin, derived from pooled human seminal plasma, possesses a molecular weight of 76.165 kDa (excluding glycosylation) and comprises 691 amino acid residues.
Physical Appearance
White, lyophilized powder after filtration.
Formulation
The LTF protein undergoes filtration (0.4 µm) and lyophilization in a solution containing 0.5 mg/ml LTF, 0.05 M phosphate buffer (pH 7.4), and 0.075 M NaCl.
Solubility
To create a working stock solution of around 0.5 mg/ml, reconstitute the lyophilized pellet with deionized water and allow complete dissolution. Note: This product is not sterile. Prior to cell culture applications, filter the solution through an appropriate sterile filter.
Stability
Store the lyophilized protein at -20°C. After reconstitution, aliquot the product to minimize freeze-thaw cycles. The reconstituted protein remains stable at 4°C for a limited period, showing no alterations for up to two weeks.
Purity
SDS-PAGE analysis confirms a purity exceeding 90%.
Human Virus Test
Samples obtained from each donor have undergone rigorous testing and are confirmed negative for HBsAg, HIV-1/2, HCV, syphilis, aHBc, and RRR.
Synonyms
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
Source
Human seminal plasma.
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
Structure and Properties
Lactoferrin is composed of a single polypeptide chain with 703 amino acid residues, folded into two globular lobes, each containing one iron-binding site . The protein can bind two molecules of iron with high affinity, which is essential for its biological functions. Lactoferrin exists in three forms: iron-free (apo-lactoferrin), monoferric (one iron molecule bound), and diferric (two iron molecules bound) .
Lactoferrin in Seminal Plasma
In seminal plasma, lactoferrin is a significant component of sperm-coating antigens. During ejaculation, lactoferrin binds to sperm, forming a protective layer that influences sperm’s physicochemical properties . This binding is facilitated by specific lactoferrin-binding molecules present in seminal plasma, which alter lactoferrin’s properties and potentially its biological activity .
Biological Functions
Lactoferrin has a wide range of biological functions, including:
- Iron Regulation: By binding iron, lactoferrin helps regulate iron availability in the body, which is crucial for various metabolic processes .
- Antimicrobial Activity: Lactoferrin exhibits antimicrobial properties by sequestering iron, which is essential for bacterial growth, and by directly interacting with microbial cell membranes .
- Immune Modulation: Lactoferrin modulates the immune response by interacting with various immune cells, including monocytes, macrophages, neutrophils, and lymphocytes .
- Anti-inflammatory Effects: Lactoferrin reduces inflammation by inhibiting the production of pro-inflammatory cytokines and by binding to lipopolysaccharides (LPS) on the surface of Gram-negative bacteria .
Clinical and Industrial Applications
Due to its diverse biological functions, lactoferrin has potential applications in various fields:
- Medical: Lactoferrin is being explored for its therapeutic potential in treating infections, inflammatory diseases, and iron deficiency anemia .
- Nutritional: Lactoferrin is added to infant formulas and dietary supplements to enhance immune function and provide antimicrobial protection .
- Cosmetic: Lactoferrin is used in skincare products for its anti-inflammatory and antioxidant properties .
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