Analytical Data
-
基因名
LPO
- Application
-
别名
LPO；SAPX；Lactoperoxidase
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P22079
-
表达区间
81-712aa
-
氨基酸序列
TRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLEVGCGAPAPVV RCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTP GKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDF APDTELGSSEYSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRA GFVCPTPPYKSLAREQINALTSFLDASFVYSSEPSLASRLRNLSSPLGLM AVNQEVSDHGLPYLPYDSKKPSPCEFINTTARVPCFLAGDSRASEHILLA TSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAFVQIITFRDYL PILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDE NYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMM TGELRNKLFQPTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQT LEELNTVLKSKMLAKKLLGLYGTPDNIDIWIGAIAEPLVERGRVGPLLAC LLGKQFQQIRDGDRFWWENPGVFTNEQKDSLQKMSFSRLVCDNTRITKVP RDPFWANSYPYDFVDCSAIDKLDLSPWASVKN
-
分子量
77 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
Related Products
Protein Description
LPO (Lacto-peroxidase) is an enzyme primarily found in various biological fluids, including saliva, milk, and tears, where it plays a crucial role in the innate immune system by participating in the antimicrobial defense mechanism. Its ability to catalyze the oxidation of thiocyanate ions in the presence of hydrogen peroxide leads to the formation of antimicrobial compounds, providing a first line of defense against pathogens. Research on LPO and its recombinant forms has gained traction due to its potential applications in food preservation, oral hygiene products, and therapeutic formulations. Advances in recombinant DNA technology allow for the production of LPO in large quantities and with specific modifications to enhance its stability and activity. Studies have focused on optimizing the expression systems, such as bacteria or yeast, for efficient production, as well as characterizing the biochemical properties of the recombinant LPO. Additionally, understanding its structural and functional dynamics has implications for developing novel antimicrobial agents. Given the rise of antibiotic resistance, the exploration of LPO's role in combatting infectious diseases and its possible incorporation into consumer products represents a significant area of interest in biochemistry and molecular biology. The continued investigation into LPO not only elucidates its functional mechanisms but also paves the way for innovative applications in health and food safety.
