Analytical Data
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基因名
LTF
- Application
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别名
LTF；Lactotransferrin
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P02788
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表达区间
1-711aa
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氨基酸序列
MKLVFLVLLFLGALGLCLAGRRRRSVQWCAVSQPEATKCFQWQRNMRKVC GPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAE VYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGRRRTAGWNVPIG TLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENK CAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELL CPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGK DKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQN LRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDC IALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDR PVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQT GSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTG AFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKR KPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDK FCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTS PLLEACEFLRK
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分子量
105 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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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.
