Analytical Data
-
基因名
textilinin
- Application
-
别名
(Txln-1)
-
种属
Pseudonaja textilis
-
表达系统
E. coli
-
标签
N- His & C- Myc
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q90WA1
-
表达区间
25-83aa
-
分子量
14.1 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
Textilinin, a novel protein derived from the venom of the spider species **Textilis** spp., has garnered significant attention in the field of biomedical research due to its unique structure and potential therapeutic applications. This protein exhibits remarkable properties, including antimicrobial and analgesic activities, making it a candidate for novel drug development. The study of textilinin is particularly relevant in the context of rising antibiotic resistance, as researchers explore its mechanisms of action to develop alternative treatments for bacterial infections. Additionally, its potential role in pain management presents opportunities for creating new analgesics that could address the opioid crisis. Recent advancements in protein engineering and recombinant DNA technology have enabled the production of textilinin in vitro, facilitating comprehensive studies on its biological functions and interactions.
Understanding textilinin's structural and functional characteristics is vital for elucidating its therapeutic potential and paving the way for innovative medical applications. Thus, ongoing research aims to harness textilinin's bioactive properties, exploring modifications that enhance its efficacy and safety profile. This could lead to significant contributions in various fields, including pharmacology, microbiology, and pain management, ultimately improving patient care and treatment outcomes.
