Analytical Data
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Gene name
LTF
- Application
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Alternative Names
LTF;Lactotransferrin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02788
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Expression Region
1-711aa
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AA Sequence
MKLVFLVLLFLGALGLCLAGRRRRSVQWCAVSQPEATKCFQWQRNMRKVC GPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAE VYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGRRRTAGWNVPIG TLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENK CAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELL CPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGK DKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQN LRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDC IALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDR PVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQT GSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTG AFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKR KPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDK FCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTS PLLEACEFLRK
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Molecular Weight
105 kDa
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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
LTF (Lactoferrin) is an iron-binding glycoprotein found primarily in mucosal secretions such as saliva, tears, and breast milk. It plays a crucial role in several physiological functions, including antimicrobial activity, immune modulation, and iron homeostasis. The significance of LTF in health and disease has prompted extensive research into its potential therapeutic applications. Studies have revealed its roles in combating infections, promoting gut health, and potentially influencing cancer progression. Additionally, LTF's ability to bind iron suggests potential use in addressing conditions associated with iron deficiency and overload. The focus on recombinant LTF (rLTF) production has emerged due to the increasing demand for large quantities of this protein for clinical and research purposes. Advances in biotechnology, particularly in the fields of protein engineering and expression systems, have enabled the development of rLTF with enhanced properties. Researchers are investigating various expression platforms, such as yeast, bacteria, and mammalian cells, to optimize yield, functionality, and stability. Understanding the structure-function relationship of rLTF is also a vital area of research, as it may guide the design of novel derivatives with improved efficacy. Overall, the exploration of LTF and its recombinant forms holds promise for innovative therapies across a spectrum of health-related issues, making it a significant focus in the realms of biochemistry and medical research.











