Analytical Data
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Gene name
Lactoferrin/LTF
- Application
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Alternative Names
HLF2; LF; GIG12; Lactotransferrin; Growth-inhibiting protein 12; Talalactoferrin; Lfcin-H; Kaliocin-1
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Species
Pig
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14632
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Expression Region
Val25~Glu348
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Molecular Weight
66kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Lactoferrin (LTF) is an iron-binding glycoprotein primarily found in milk and other secretions, known for its multifunctional roles in the immune system, iron metabolism, and antimicrobial activity. Research into recombinant lactoferrin has gained prominence due to its potential therapeutic applications, particularly in enhancing immune responses and acting as a natural antibacterial agent. The development of recombinant LTF involves the use of genetic engineering techniques to produce this protein in various host systems, allowing for better yields and more accessible production compared to traditional extraction methods from natural sources. Investigations into its structure-function relationships aim to elucidate the mechanisms by which LTF exerts its biological effects, while studies exploring its use in dietary supplements and functional foods highlight its potential benefits in promoting gut health and overall well-being. The growing interest in the health benefits associated with lactoferrin has positioned it as a key target for biotechnological advancements, fueling research initiatives that seek to harness its properties for clinical applications in immunology and nutrition. Moreover, the rising prevalence of antibiotic resistance has further underscored the need for alternative antimicrobial agents like lactoferrin, making its study increasingly relevant in the context of public health.
