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Manufactured by BioVendor

Lactoferrin NATIVE, Human Breast Milk

  • Regulatory status:RUO
  • Type:Native protein
  • Source:Human breast milk
  • Other names:Lactotransferrin, Talactoferrin
  • Species:Human
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Cat. No. Size Price


RD1663441000 1 mg
PubMed Product Details
Technical Data

Type

Native protein

Description

Native protein isolated from Human Breast Milk, 691 AA, MW 76,165 kDa (calculated without glycosylation). Protein identity confirmed by LC-MS/MS (NCBI no. gi|119585171).

Amino Acid Sequence

GRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK

Source

Human breast milk

Purity

Purity as determined by densitometric image analysis: >95%

SDS-PAGE Gel

SDS-PAGE analysis of Lactoferrin NATIVE protein, 12% gel stained with Coomassie Brillant Blue G250

  1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
  2. reduced and boiled sample, 2.5ug/lane
  3. non-reduced and non-boiled sample, 2.5μg/lane

Endotoxin

< 0.1 EU/μg

Formulation

Filtered (0.4 μm) and lyophilized from 1 mg/ml solution in phosphate buffered saline pH 7.4

Reconstitution

Add deionized water to prepare a working stock solution of approximately 1.0 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Applications

Western blotting, ELISA, Cell culture and/or animal studies, Immunological methods

Shipping

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

Storage/Expiration

Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.
LC-MS/MS to identify the protein and determine purity of the protein.
SDS PAGE to determine purity of the protein.
LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

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

Summary

"Lactoferrin (also called lactotransferrin) is a glycoprotein with a molecular weight of about 80 kDa, which was classified as a member of the transferrin family, due to its 60% sequence identity with serum transferrin. Higher levels of lactoferrin were found in colostrum and mature milk. Lactoferrin has been also found in most mucosal secretions such as uterine fluid, vaginal secretion, seminal fluid, saliva, bile, pancreatic juice, small intestine secretions, nasal secretion, and tears. Lactoferrin belongs to the innate immune system. Apart from its main biological function, namely binding and transport of iron ions, lactoferrin also has antibacterial, antiviral, antiparasitic, catalytic, anti-cancer, anti-allergic and radioprotecting functions and properties."

Summary References (26)

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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