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Lactoferrin Powder 1.195g/Cm3 Weight Loss Supplement Powder

Lactoferrin Powder 1.195g/Cm3 Weight Loss Supplement Powder

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    Lactoferrin Powder


    1.195g/Cm3 Weight Loss Supplement Powder


    CAS No 112163-33-4

  • Brand Name
    Kan Ying
  • Purity
  • Product Name
    Joro Spider Toxin
  • Color
    White Powder
  • Storage
    Cool Dry Place
  • CAS No
  • Shelf Life
    2 Years
  • Boiling Point
    979.9ºC At 760mmHg
  • Point Of Flammability
  • Density
  • Place of Origin
  • Brand Name
    Kan Ying
  • Minimum Order Quantity
  • Price
    To discuss
  • Packaging Details
  • Delivery Time
  • Payment Terms
    L/C, D/A, D/P, T/T, Western Union, MoneyGram,Dollars
  • Supply Ability

Lactoferrin Powder 1.195g/Cm3 Weight Loss Supplement Powder

lactoferrin Bacteriostatic agent Weight Loss Powder anti-inflammatory


1.  Product title:  Joro spider toxin


2.  Pictures of the product:


Product Name lactoferrin Specification 99%
Appearance White powder Main Effect Bacteriostatic agent
Brand Name Kan Ying Store-method Cool Dry Place
Shelf Life 2 Years When
Properly Stored
From India



3. Product Description:Lactoferrin is widely distributed in human and mammal milk and various other tissues and their secretions (including internal and external secretions such as tears, semen, bile, synovial fluid, and neutrophils), but the content in milk is relatively high. High [10], among which the content of lactoferrin in bovine colostrum is the highest. The lactoferrin in the blood is mainly secreted by multinucleated cells. The bone marrow, salivary glands and endometrium can also secrete a small amount of lactoferrin [4].
The concentration of lactoferrin in human milk is about 1.0-3.0mg/mL, which is 10 times that in cow milk (the content in cow's milk is 0.02-0.35mg/mL), and accounts for 20% of the total protein of normal breast milk. During lactation, lactoferrin The protein content changes with the time of lactation. For example, the lactoferrin in human colostrum can reach 6-14mg/mL, and the lactoferrin drops to 1mg/mL during normal lactation. The lactoferrin content in colostrum of cows can reach 1mg/mL on the first day after delivery. When the content of lactoferrin in milk cow's milk will rise again at the end of lactation [4]. Lactoferrin (bovine) is a polypeptide chain with 703 amino acid residues, which folds into two basically symmetrical and highly homologous leaf-like structures (N-leaf and C-leaf) [5]. Studies have shown that this structure may have formed due to gene overlap during evolution. The N-leaf structure contains amino acids 1 to 332, and the C-leaf structure contains amino acids 344 to 703. The two structures are linked by a hinge region, each of which is about 40kDa in size. N-leaf and C-leaf can be divided into N1, N2 area and C1, C2 area correspondingly. N-leaf carries higher positive charge than C-leaf. The N-lobe structure has been confirmed to be related to the improvement of the antibacterial activity of lactoferrin, and the C-lobe structure can play a role in the treatment of gastric disease, diabetes and corneal injury. Lactoferrin has two metal ion binding sites, each site contains two tyrosine, one aspartic acid and one histidine, which can reversibly bind one Fe3+ ion and one CO32- ion. Because the complex of lactoferrin and iron ions is red, it is also called "globin" [3].
Physical and chemical properties
Lactoferrin has a high affinity for iron ions, which is 250 to 300 times that of transferrin. According to the difference in binding iron ions, lactoferrin can be divided into three types: iron-deficient type, iron half-saturated type and iron-saturated type. Different types of lactoferrin have different resistance to pasteurization and heat denaturation. Among them, the iron-saturated type has the strongest resistance and the iron-deficiency type has the weakest resistance. Lactoferrin can not only combine with Fe3+ and Fe2+, but also with Cu2+, Mn2+, and Zn2+ [3].
Regarding the thermal stability of lactoferrin, studies have found that heat treatment at 72°C for 20s or 135°C for 8s hardly affects the iron binding capacity of lactoferrin, but if the treatment time at the two temperatures is prolonged, the iron binding will be reduced. ability. The heat treatment intensity at 85°C for 10 minutes will not affect the antibacterial activity of lactoferrin. In addition, studies have shown that under the conditions of pH 2.0 or pH 3.0, after treatment at 120°C for 5 minutes, lactoferrin is degraded, but the antibacterial activity of the degradation products is higher than before treatment. The results of this experiment led people to discover the existence of lactoferrin active peptides. Lactoferrin has antibacterial effects on both gram-positive bacteria and gram-negative bacteria, but it has a stronger effect on gram-negative bacteria. The iron saturation of lactoferrin is negatively correlated with bacteriostasis. Environmental pH changes affect the inhibitory effect of lactoferrin on gram-positive bacteria, but have little effect on gram-negative bacteria. When the pH is between 7.5 and 8.0, the antibacterial effect is the best. The antibacterial activity of lactoferrin after pasteurization below 70℃ has no effect; the increase of HCO3-concentration is beneficial to enhance its antibacterial activity [3].


5. Biological function:Lactoferrin can respond to various physiological and environmental changes, so it is considered a key component of the innate defense system. Lactoferrin shows strong antibacterial activity against a variety of bacteria, fungi, yeasts, viruses and parasites. It also has anti-inflammatory and anti-cancer activities, and has a variety of enzyme functions. Lactoferrin plays a key role in maintaining cellular iron levels in the body [5].
Antibacterial activity
The first discovered and widely studied biological function of lactoferrin is its antibacterial ability. Lactoferrin has a broad spectrum of resistance to Gram-positive bacteria, Gram-negative bacteria and fungi, and can effectively inhibit the growth of Escherichia coli, Salmonella typhi, Streptococcus, Legionella pneumophila, and Staphylococcus aureus. Clinically, after oral lactoferrin treatment is given to patients, the infection of gastrointestinal bacteria is reduced, but the growth of Lactobacillus and Bifidobacteria is not affected [3].
It is generally believed that lactoferrin competitively deprives the iron element required for bacterial growth by chelating iron ions, thereby inhibiting the growth of bacteria. Studies have also shown that lactoferrin can bind to lipid A and promote the separation of lipid A from the bacterial wall of Gram-negative bacteria, leading to bacterial death. There is a sequence encoding lactoferrin at the N-terminus of lactoferrin, and lactoferrin is an antibacterial peptide with natural antibacterial activity [3].
Antiviral activity
Lactoferrin can help the body resist a variety of viral infections. Intestinal infections caused by rotavirus, enterovirus and adenovirus can all be treated with lactoferrin. In the early stage of infection, lactoferrin can inhibit the replication of adenovirus and prevent the virus from adsorbing to target cells to prevent infection . When studying the Norovirus that causes infectious diarrhea, it was found that lactoferrin can reduce cytotoxic damage, reduce the number of virus cells, prevent virus-cell adhesion, inhibit virus replication, and increase the expression of antiviral cytokines. So as to kill the norovirus. Lactoferrin can inhibit the activity of HIV-1 reverse transcriptase and splicing enzyme and prevent HIV virus from infecting cells. In addition, lactoferrin can also resist the invasion of the body by viruses such as HSV-1, HCMV, and HCV. There is also a view that lactoferrin has no direct antiviral effect, but indirectly through the antiviral response of the immune system to achieve the purpose of antiviral [3].
Antifungal activity
Human lactoferrin, bovine lactoferrin and lactoferrin-derived peptides all have in vitro activity against human pathogenic fungi (especially Candida albicans and several other Candida species). Like anti-bacteria, lactoferrin can kill Candida albicans and Clostridium crusii by changing the permeability of the cell surface. Lactoferrin can change the permeability of the cytoplasm and mitochondrial membrane of Cryptococcus neoformans and Candida albicans. The antifungal mechanism of lactoferrin is achieved through interaction with the cell surface rather than iron deprivation [5].
In recent years, the anti-cancer effect of lactoferrin has been widely reported. Oral administration of bovine lactoferrin to rodents can inhibit the formation of tumors induced by chemical methods. Clinical trials have confirmed that lactoferrin can inhibit the occurrence and development of tumors. Lactoferrin has the ability to regulate the production of cytokines in cancer. Lactoferrin induces apoptosis in vitro and prevents tumor growth. It can also prevent the transition from G1 to S during the cell cycle of malignant cells. In addition, treatment of mouse tumors with recombinant human lactoferrin can inhibit tumor growth, increase the level of anti-cancer factors (such as IL-18), and activate NK cells and CD8+ T lymphocytes. Recently, clinical trials have shown that bovine lactoferrin can inhibit colorectal cancer, while human lactoferrin can reduce the risk of colon cancer. For breast cancer, lactoferrin can inhibit the growth of its tumor cells. Adding exogenous lactoferrin to the medium of breast cancer cell line (MDA-MB-231) will cause cell cycle arrest in the G1/S transition period. In addition, lactoferrin induced growth arrest of Smad-2 in HeLa cells. Although the results obtained by the researchers indicate that lactoferrin has obvious anti-tumor effects, the mechanism by which it exerts these effects is not fully understood [5].
Immunomodulatory and anti-inflammatory activity
Because lactoferrin is widely distributed in the body's exocrine fluid, it can be used as the body's first natural immune barrier to participate in immune regulation. Lactoferrin is one of the important inflammatory response regulators and an important component involved in regulating the immune system. It can protect the body against microbial infections, reduce the incidence of E. coli and infectious diarrhea, and improve the growth of newly weaned piglets . For newborns with immature immune systems, colostrum rich in lactoferrin can help activate and regulate the function of the immune system, and at the same time promote the rapid establishment of their own immune system. Oral bovine lactoferrin increases the number of lymph nodes and spleen cells, increases the activity of peritoneal macrophages and splenic NK cells, and enhances the production of IL-12 and IFY-γ and other cytokines in Th1 T cells. Lactoferrin inhibits the programmed cell death of immune cells by blocking the passage of apoptosis signals; it can also regulate the maturation and differentiation of T lymphocytes and the balance of Th1/Th2 cytokines through the interaction with antigen layer delivery cells [3].
Enzyme activity
Lactoferrin can act as an enzyme in certain catalytic reactions. Certain motifs between lactoferrin and ribonuclease A have significant similarities. Lactoferrin has DNA binding characteristics and can play a role in the transcriptional activation of specific DNA sequences or as a signal transduction mediator. Among all milk proteins, lactoferrin has the highest amylase and ATPase activities, however, they are not the only enzymatic activity. The various activities exhibited by lactoferrin are attributed to the changes in its protein properties. Lactoferrin has a variety of isoforms, different degrees of glycosylation, different tertiary structures and degrees of oligomerization[5] .


6. Separation method:Traditional method
There are many ways to purify lactoferrin, and many companies choose cation exchange chromatography systems to obtain lactoferrin in a wide range. The separation and purification of lactoferrin began in the 1980s, and many companies are committed to developing processes for obtaining high-purity lactoferrin. The methods of separation and purification of lactoferrin range from initial cation exchange to affinity chromatography to immunological methods, and the combination of various methods has advantages and disadvantages for the separation and purification of lactoferrin [6].
Cation exchange chromatography. The use of cation exchange chromatography to separate lactoferrin from raw materials is a traditional method, which has the advantages of simple operation, few steps, continuous sample injection and easy expansion. However, traditional chromatographic chromatography has many disadvantages when it is used to quickly and massively recover lactoferrin from whey protein, such as contamination of chromatographic materials, long cycle time, high pressure when droplets pass through the column, and complexity In addition, many miscellaneous proteins with the same and similar isoelectric points as lactoferrin in the raw materials are eluted together during the separation and purification of lactoferrin, so the obtained lactoferrin has low purity and high cost. And relatively low yield [6].
Membrane adsorption. Due to the poor thermal stability of lactoferrin, membrane separation is a separation process that does not require heating, phase change, and does not require chemical reagents. Therefore, this method can maintain the biological activity of lactoferrin to the utmost extent, making it an advantage for the separation and recovery of lactoferrin. Kerstin Plate et al. studied whether membrane technology can be used to recover lactoferrin from whey and whether laboratory-level equipment can be directly applied to industrialization. The membrane area used in the test rose from 15cm2 to 4m2. The test results show that the best condition is to use the Sartobind S system, the membrane area is expanded to 2m2, and no cleaning is required for 8 cycles. Almécija et al. used a 300 kDa ceramic microporous membrane to separate Lf from whey. The study showed that the optimal solution pH for obtaining lactoferrin is 5 and 10, respectively. The former can obtain lactoferrin, while the latter can make lactoferrin. Remains in the original whey. In order to overcome the disadvantage of membrane adsorption that the approximate molecular weight cannot be distinguished, Brisson et al. used a combination of a charged membrane and an electric field. The electric field played an important role in the movement of the protein. Although part of the purity problem was solved, the electrolysis reaction on the surface of the solution had an impact on Lf. Separation has a negative effect [6].
Electric separation. Electro-separation technology is a technology that uses the difference in molecular size and its own charge to separate protein molecules. Electric current can speed up the separation. Compared with the traditional pressure-driven method, the application of electric field has the advantage of increasing the speed of lactoferrin separation, but at the same time reducing its purity. The reason is that the migration of other whey proteins and protein-protein interactions while separating Lf. The combination of electric separation and microfiltration membrane can overcome the disadvantages of low selectivity and solution contamination. N Ndiaye et al. used this method to separate lactoferrin. The optimal separation condition for lactoferrin is pH=3.0. When 2 g/L KCl solution is used as the solution, the optimal condition is 1.5×10-8m2/ (V·s); When deionized water is used as the solution, the best condition is 3.0×10-8m2/(V·s). Combined with a 500 kDa ultrafiltration membrane, after 4 hours of treatment, the migration rate reached 46% and the yield was 15%. The disadvantage of this method is that at pH=3.0, β-lactoglobulin will also be separated out [6].
new method
Due to the wide application of lactoferrin, people have higher and higher requirements for its purity, but some proteins in whey, such as lactoperoxidase, have similar molecular weights and isoelectric points to lactoferrin. In addition, some scholars also pointed out that the lactoferrin binding protein was purified at the same time as the lactoferrin, including ribonuclease-4, angiogenin, neutrophil gelase-related calpoprotein and fibroblasts. Cell growth factor binding protein, etc. These trace proteins and lactoferrin may be involved in many physiological activities of lactoferrin in vivo. Conventional hydrophobic interaction, affinity chromatography, molecular exclusion, ultrafiltration, and membrane filtration are complex processes, coupled with low selectivity, so some methods with high selectivity have been developed [6].
Hydroxyapatite method. Paul K Ng et al. used a mixed mode chromatography-ceramic hydroxyapatite chromatography. This method can separate Lf, Lp and other globulins in whey in one step, and then obtain Lf through gradient elution. The test results show that an 80 L hydroxyapatite column can collect 0.32 kg of Lf in one hour, and the obtained Lf has been verified to contain no Lp activity. The high yield, low cost, and simple steps make this operation possess all the characteristics for an effective large-scale biotechnology industry. The purification process of hydroxyapatite requires a lot of water to effectively separate macromolecules. The product recovery rate depends on the amount of buffer used. This method cannot distinguish molecules with similar hydrated particle size, so the purity of the product may be affected. In addition, the interaction between different proteins in whey makes this process difficult to predict [6].
Phage protein-affinity chromatography. Affinity columns are generally based on antigen-antibody reactions, and ligands with specific binding are widely used for different separation and purification purposes. The choice of affinity column is good for obtaining high purity protein. However, the ligand itself is expensive. According to the separation of different target proteins, the ligand itself needs to be screened and purified again. The fragility of the ligand reduces the service life of the column. Ligand degradation leads to product contamination, as well as ingredient leakage and toxicity issues that limit its application. Phage, as a multi-ligand expressor, has a large library and has been successfully bred for phages such as lactoferrin, insulin and serum albumin. The peptide ligands in affinity chromatography can be immobilized on the substrate by conventional methods or solid-phase direct synthesis methods for the separation and purification of the target protein. Artificially synthesized peptides and host-expressed peptides often show different performance. Therefore, Wim Noppe and others have successfully bred 4 strains of phage that can bind to Lf hexapeptide, and then directly immobilized the 1 μm phage on a macroporous matrix. Used for the separation and purification of Lf. The experiment showed that the affinity method can be used to extract Lf in one step, and its purity is higher than 95%. The advantages of this method are that the matrix holes are not easy to be blocked, the operation process is simple, sustainable, and the recovery speed is fast. In addition, phage expression is cheaper and simpler than monoclonal antibodies [6].
Magnetic nanoparticles. The advantage of using magnetic nanoparticles to separate Lf is that when an electric field is applied, the magnetic nanoparticles instantly become magnetic and can swim under the action of the electric field. When the applied electric field is removed, the magnetism disappears immediately, which is conducive to the separation of magnetic nanoparticles, and then combined with membrane and other technologies, the target protein is finally obtained. Bo-Hung Lai et al. combined Concanavalin A on Fe3O4 magnetic nanoparticles and obtained nearly superparamagnetic particles with an average diameter of (11.74±3.86) nm. Experiments have proved that the optimal conditions for the particle separation of Lf are pH=7, temperature 25 ℃, equilibrium time within 5 min, maximum adsorption capacity and equilibrium constant are 59.2 mg/g and 0.010 3 L/mg, respectively . Lin Chen et al. used heparin as an affinity ligand to separate Lf with a magnetic affinity method. The binding capacity of heparin to Lf was 0.92 mg/g. In the experiment, NaCl was used as the eluent to recover Lf from acidic whey very efficiently through a one-step method. The highest binding capacity was 164 mg/g. And the purity of the obtained Lf is higher than commercial standards. The comparative competitive adsorption test proves that the magnetic method is a potential method for rapid and large-scale production [6].


7. application:The extensive biological functions of lactoferrin determine its application in cosmetics, food, animal production, medical and other fields, and can be used as antioxidants, immune boosters, iron supplements, drug carriers, etc. [7].
Lactoferrin is a natural substance in the human body. It has a wide range of antibacterial, anti-inflammatory, melanin inhibition and collagen formation effects, so it can be used as an effective ingredient in the development and utilization of cosmetic preparations. In the development of whitening cosmetics, the raw materials have certain stability during processing, and lactoferrin has extremely high stability and can be used as raw materials for processing into whitening agents. Studies have shown that using lactoferrin to identify whitening functions on animal skin models, lactoferrin can reduce the formation of melanin, and the ability to inhibit melanin is directly proportional to the content of lactoferrin, which indicates that lactoferrin can be The skin absorbs, thus playing a whitening role. Lactoferrin can promote the collagen synthesis of osteoblasts in the human body, make up for the loss of collagen in the body due to age factors and environmental factors, and have a whitening effect on human skin. The whitening effect of lactoferrin is remarkable, and the application of cosmetics has a broad prospect, but its molecular mechanism needs to be further studied [7].
food industry
As of 2021, there are many products containing lactoferrin on the market, including yogurt, skimmed milk, health food and fermented dairy products. At the end of the 20th century, Japanese dairy products companies began to produce and sell lactoferrin-containing infant formula milk powder. The benefits of adding lactoferrin to infant milk powder include promoting iron absorption and improving intestinal flora. And so on. It has been confirmed in clinical and animal tests that these lactoferrin-containing products are very beneficial to health. It is popular in Japan, South Korea and other countries and regions to add lactoferrin to fermented dairy products, baby food, soy protein products, and meat products to supplement lactoferrin, enhance the body’s immunity, and prevent the body from contracting viral colds and intestinal infections. And other diseases [7].
Animal production
When lactoferrin is added to the feed of sows, sows can obtain a large amount of endogenous lactoferrin, which can reduce the probability of iron deficiency anemia in piglets, improve the immunity of piglets, and promote the growth of piglets. Adding lactoferrin to the piglet’s diet can improve the piglet’s intestinal microflora, prevent intestinal diarrhea, and enhance the piglet’s intestinal absorption of nutrients. The feed with lactoferrin can prevent the feed from being oxidized and decomposed, and at the same time enhance the nutrient content of the feed. Lactoferrin also has the function of better maintaining its physiological functions during high-temperature processing of feed, so it can be used as a green feed additive for animal feeding [7].
Lactoferrin not only regulates the body's iron metabolism, but also plays an important role in the body's anti-inflammatory and antioxidant properties. Lactoferrin receptors exist on the surface of cell membranes with a molecular weight of about 105 kDa. Common target cells include mucosal epithelial cells, liver cells, monocytes, macrophages, lymphocytes, etc., Staphylococcus aureus and Pseudomonas, etc. bacterial. Lactoferrin binds to bacterial cell surface receptors, can activate intracellular signal pathways or enter the nucleus through endocytosis, and participate in immune and antibacterial functions. Studies have confirmed that lactoferrin receptors are highly expressed in neurons and capillary endothelial cells in the brains of patients with Parkinson's disease, and that lactoferrin binds to it to inhibit the spread of prion protein; this effect of lactoferrin suggests that it is neurodegenerative The potential application value of disease prevention and treatment [7].


8. Detection method:As of 2021, the reported detection methods of lactoferrin include enzyme-linked immunoassay, high performance capillary electrophoresis, biosensor assay, high performance liquid chromatography, high performance liquid chromatography and mass spectrometry, etc. [8].
Enzyme-linked immunoassay is a detection method based on the specific reaction of antigen and antibody, which has the advantages of sensitive reaction and strong specificity. Coat the anti-lactoferrin antibody (primary antibody) in the microtiter plate. After adding the target lactoferrin, the lactoferrin binds to the primary antibody, and then the lactoferrin antibody (secondary antibody) is added to form a sandwich structure, and finally Add a color reagent, use a microplate reader to measure the absorbance value of a specific wavelength, and the absorbance value is proportional to the lactoferrin content, and a standard curve can be drawn to achieve the purpose of quantitatively detecting the lactoferrin concentration in the sample. Although the enzyme-linked immunosorbent assay is highly sensitive, it usually requires multiple incubations, washings and cleanings. The operation is cumbersome, and the antibodies and anti-antibodies used are difficult to prepare, expensive, and not suitable for mass sample analysis [8].
High performance capillary electrophoresis
The smaller the sample molecular diffusion coefficient or the larger the molecular weight, the higher the separation efficiency of the capillary column. Most high-efficiency capillary electrophoresis methods use quartz capillaries as the separation channel, and use high-voltage direct current electric fields as the drive to achieve the purpose of liquid phase separation. It has the advantages of simple operation and high sensitivity, but it needs to solve the adsorption of the capillary wall to the target substance lactoferrin. The problem of poor repeatability is caused, and the test results are greatly affected by the complex matrix of the sample [8].
Surface Plasmon Resonance Technology
The incident light incident on the interface of two metal media with different refractive index at a critical angle can cause the metal to produce free electronic resonance. The electron absorbs the light energy and greatly weakens the reflected light, and the incident angle that can make the reflected light completely disappear within a certain angle is called the incident angle Is the SPR angle. The SPR angle changes with the change of the refractive index of the medium surface, and the change of the refractive index is directly proportional to the mass of the molecules bound to the surface of the medium. Therefore, the specific signal of the interaction between biomolecules can be obtained by the dynamic change of the SPR angle during the biological reaction. To achieve the purpose of detection. The biosensing immunoassay based on surface plasmon resonance technology can automatically detect low-content lactoferrin in real time without labeling, but the experimental temperature and sample composition affect the measurement results, and the cost of equipment is relatively expensive [8].
High performance liquid chromatography
High performance liquid chromatography (HPLC) is a technique that uses different chromatographic columns to separate different components due to the difference in partition coefficient and adsorption capacity, and is recognized by the detector. It consists of a non-polar stationary phase and a polar flow. The reversed-phase high performance chromatography of the liquid chromatography system composed of phases is the most widely used liquid chromatography method in HPLC. The advantages are sensitive reaction, accurate and reliable results, and good repeatability, but the disadvantage is that the purity of the sample is higher. , Often need to go through a complicated pre-treatment process before sampling [8].
High performance liquid phase-mass spectrometry
The mass spectrometer measures the mass-nucleus ratio of specific ions to accurately characterize the analyte, and is usually combined with high-performance liquid chromatography or gas chromatograph to achieve precise quantification. Because the molecular weight of protein is too large, in the analysis of protein, it is usually hydrolyzed into a mixture of peptides by various means such as trypsin, and then the protein is detected by the determination of specific peptides in it. There are reports that researchers combine proteomics technology, isotope labeling technology and high performance liquid chromatography-mass spectrometry to detect lactoferrin in dairy products. Liquid-phase mass spectrometry results are sensitive and reliable, high reproducibility, and high recovery rate. However, it is necessary to break large protein molecules into small amino acid molecules, and use specific amino acid fragments for qualitative and quantitative determination. At this time, the protein has been deformed, which is not conducive to the test. To determine whether the lactoferrin is active in the sample, and the equipment is expensive, the professional requirements of the operator are higher [8].


9. Pictures of the product: 

Lactoferrin Powder 1.195g/Cm3 Weight Loss Supplement Powder 0Lactoferrin Powder 1.195g/Cm3 Weight Loss Supplement Powder 1