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Manufactured by BioVendor

Lactoferrin Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Lactotransferrin, Talactoferrin
  • Species:Human
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Cat. No. Size Price


RD194334200R 96 wells (1 kit)
PubMed Product Details
Technical Data

Notice

For processing the stool samples we recommend using BioVendor Extraction Buffer. The reagent is not included and can be ordered separately (Cat. No.: C005821, 100 ml)
Special Dilution Buffer is needed for measurement of human lactoferrin in stool extract and is not included.

Please find the protocol for preparation and analysis of stool extracts in Docs.

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Plasma-EDTA, Urine, Cerebrospinal fluid, Bronchoalveolar lavage, Milk, Saliva, Stool

Sample Requirements

Serum, Plasma (EDTA), BALF, Breast milk, Saliva: 5 µl/well

CSF, Urine, Stool extract: 20 µl/well

  • For processing the stool samples we recommend using BioVendor Extraction Buffer. The reagent is not included and can be ordered separately (Cat. No.: C005821, 100 ml)
  • Special Dilution Buffer is needed for measurement of human lactoferrin in stool extract and is not included.
    For protocol for preparation of stool extracts and other details, please contact us at info@biovendor.com

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box)

Calibration Curve

Calibration Range

2.5–80 ng/ml

Limit of Detection

1.1 ng/ml

Intra-assay (Within-Run)

n = 8; CV = 3.3 %

Inter-assay (Run-to-Run)

n = 6; CV = 5.4 %

Spiking Recovery

Serum: 96.6 %
Plasma (EDTA): 103.2 %
BALF: 104.7 %
CSF: 102.3 %
Urine: 104.4 %
Stool extract: 89.7 %

Dilutation Linearity

Serum: 94.6 %
Plasma (EDTA): 97.5 %
BALF: 88.3 %
CSF: 99.5 %
Urine: 98.4 %
Breast milk: 97.1 %
Saliva: 97.1 %
Stool extract: 94.9 %

Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3.5 hours
  • The kit measures lactoferrin in serum, plasma (EDTA), bronchoalveolar lavage fluid (BALF), cerebrospinal fluid (CSF), urine, breast milk, saliva and stool extract
  • Special Dilution Buffer is needed for measurement of human lactoferrin in stool extract and is not included. For protocol for preparation of stool extracts and other details, please contact us at info@biovendor.com
  • Assay format is 96 wells
  • Standard is native protein based
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Bone and cartilage metabolism, Immune Response, Infection and Inflammation, Inflammatory bowel disease, Iron metabolism

Summary

Lactoferrin is 703-amino acid iron-binding glycoprotein that belongs to the transferrin family. Lactoferrin capability of binding iron is two times higher than that of transferrin. Two ferric ions can be bound by one lactoferrin molecule. There are three forms of lactoferrin according to its iron saturation: apolactoferrin (iron free), monomeric lactoferrin (one ferric ion), and hololactoferrin (binds two Fe3+ ions). The tertiary structure of hololactoferrin and apolactoferrin is different.
Lactoferrin was originally isolated from breast milk and subsequently was identified in secretions from exocrine glands and in specific granules of neutrophils. Neutrophils after degranulation are main source of lactoferrin in blood plasma. Lactoferrin has been found in most mucosal secretions such as uterine fluid, saliva, bile, pancreatic juice, small intestine secretions, nasal secretion, and tears. Lactoferrin is also present in urine and fecal samples, though levels in these samples are relatively low. The kidney produces lactoferrin in a highly ordered manner but only a minor fraction of the protein is secreted into urine. The biological properties of lactoferrin are mediated by specific receptors on the surface of target cells and can be found, for example, on mucosal epithelial cells, hepatocytes, monocytes, macrophages, polymorphonuclear leukocytes, lymphocytes, thrombocytes, fibroblasts, and on some bacteria.
Lactoferrin possesses various biological functions including its roles in iron metabolism, cell proliferation and differentiation, and antibacterial, antiviral, and antiparasitic activity. Many of these functions do not appear to be connected with its iron binding ability. During most inflammatory reactions lactoferrin concentration increases in all biological fluids, and several authors classify lactoferrin as an acute-phase protein. However, the relationship between its concentration and physiological or pathological effects on body functions is not yet well characterized. Lactoferrin has even been reported to inhibit the development of experimental metastases in mice. Lactoferrin has also been identified as a potent anabolic factor affecting osteocytes, where it induces osteoblast proliferation, survival, differentiation, reduces apoptosis of osteoblasts by 50-70% and inhibits osteoclast formation. The influence of lactoferrin on lipid metabolism was discovered through animal studies. Oral administration of bovine lactoferrin reduced plasma cholesterol levels and retarded hepatic lipid accumulation in mice and decreased serum TAG to 72% of the control level in rats. Another study of abdominally obese men and women showed that ingestion of lactoferrin reduced visceral fat.[14] Fecal lactoferrin level has investigated for its use as a non-invasive marker in the distinction of inflammatory bowel disease (IBD) and non-inflammatory condition.

References to Product

References

  • Jung HC, Seo MW, Lee S, Kim SW, Song JK. Vitamin D₃ Supplementation Reduces the Symptoms of Upper Respiratory Tract Infection during Winter Training in Vitamin D-Insufficient Taekwondo Athletes: A Randomized Controlled Trial. Int J Environ Res Public Health. 2018;15(9):2003. Published 2018 Sep 14. doi:10.3390/ijerph15092003
References to Summary

References to Lactoferrin

  • Abrink M, Larsson E, Gobl A, Hellman L. Expression of lactoferrin in the kidney: implications for innate immunity and iron metabolism. Kidney Int. 2000 May;57 (5):2004-10
  • Actor JK, Hwang SA, Kruzel ML. Lactoferrin as a natural immune modulator. Curr Pharm Des. 2009;15 (17):1956-73
  • Aisen P, Leibman A. Lactoferrin and transferrin: a comparative study. Biochim Biophys Acta. 1972 Feb 29;257 (2):314-23
  • Antonsen S, Wiggers P, Dalhoj J, Blaabjerg O. An enzyme-linked immunosorbent assay for plasma-lactoferrin. Concentrations in 362 healthy, adult blood donors. Scand J Clin Lab Invest. 1993 Apr;53 (2):133-44
  • Baynes RD, Bezwoda WR. Lactoferrin and the inflammatory response. Adv Exp Med Biol. 1994;357:133-41
  • Bennett RM, Mohla C. A solid-phase radioimmunoassay for the measurement of lactoferrin in human plasma: variations with age, sex, and disease. J Lab Clin Med. 1976 Jul;88 (1):156-66
  • Bezault J, Bhimani R, Wiprovnick J, Furmanski P. Human lactoferrin inhibits growth of solid tumors and development of experimental metastases in mice. Cancer Res. 1994 May 1;54 (9):2310-2
  • Birgens HS. Lactoferrin in plasma measured by an ELISA technique: evidence that plasma lactoferrin is an indicator of neutrophil turnover and bone marrow activity in acute leukaemia. Scand J Haematol. 1985 Apr;34 (4):326-31
  • Boxer LA, Coates TD, Haak RA, Wolach JB, Hoffstein S, Baehner RL. Lactoferrin deficiency associated with altered granulocyte function. N Engl J Med. 1982 Aug 12;307 (7):404-10
  • Brock JH. Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the newborn infant. Arch Dis Child. 1980 Jun;55 (6):417-21
  • Brock JH. The physiology of lactoferrin. Biochem Cell Biol. 2002;80 (1):1-6
  • Devi AS, Das MR, Pandit MW. Lactoferrin contains structural motifs of ribonuclease. Biochim Biophys Acta. 1994 Apr 13;1205 (2):275-81
  • Gonzalez-Chavez SA, Arevalo-Gallegos S, Rascon-Cruz Q. Lactoferrin: structure, function and applications. Int J Antimicrob Agents. 2009 Apr;33 (4):301.e1-8
  • Jenssen H, Hancock RE. Antimicrobial properties of lactoferrin. Biochimie. 2009 Jan;91 (1):19-29
  • Kanyshkova TG, Buneva VN, Nevinsky GA. Lactoferrin and its biological functions. Biochemistry (Mosc). 2001 Jan;66 (1):1-7
  • Legrand D, Elass E, Carpentier M, Mazurier J. Lactoferrin: a modulator of immune and inflammatory responses. Cell Mol Life Sci. 2005 Nov;62 (22):2549-59
  • Levay PF, Viljoen M. Lactoferrin: a general review. Haematologica. 1995 May-Jun;80 (3):252-67
  • Naot D, Grey A, Reid IR, Cornish J. Lactoferrin--a novel bone growth factor. Clin Med Res. 2005 May;3 (2):93-101
  • Niemela A, Kulomaa M, Vija P, Tuohimaa P, Saarikoski S. Lactoferrin in human amniotic fluid. Hum Reprod. 1989 Jan;4 (1):99-101
  • Ono T, Murakoshi M, Suzuki N, Iida N, Ohdera M, Iigo M, Yoshida T, Sugiyama K, Nishino H. Potent anti-obesity effect of enteric-coated lactoferrin: decrease in visceral fat accumulation in Japanese men and women with abdominal obesity after 8-week administration of enteric-coated lactoferrin tablets. Br J Nutr. 2010 Dec;104 (11):1688-95
  • Steijns JM, van Hooijdonk AC. Occurrence, structure, biochemical properties and technological characteristics of lactoferrin. Br J Nutr. 2000 Nov;84 Suppl 1:S11-7
  • Suzuki YA, Lonnerdal B. Characterization of mammalian receptors for lactoferrin. Biochem Cell Biol. 2002;80 (1):75-80
  • Takeuchi T, Shimizu H, Ando K, Harada E. Bovine lactoferrin reduces plasma triacylglycerol and NEFA accompanied by decreased hepatic cholesterol and triacylglycerol contents in rodents. Br J Nutr. 2004 Apr;91 (4):533-8
  • Tamano S, Sekine K, Takase M, Yamauchi K, Iigo M, Tsuda H. Lack of chronic oral toxicity of chemopreventive bovine lactoferrin in F344/DuCrj rats. Asian Pac J Cancer Prev. 2008 Apr-Jun;9 (2):313-6
  • Valenti P, Antonini G. Lactoferrin: an important host defence against microbial and viral attack. Cell Mol Life Sci. 2005 Nov;62 (22):2576-87
  • Ward PP, Paz E, Conneely OM.
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