Analytical Data
-
基因名
tig
- Application
-
别名
tig；PEIG1；TIG1；Retinoic acid receptor responder Protein 1
-
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
B7UJQ9
-
表达区间
1-432aa
-
氨基酸序列
MQVSVETTQGLGRRVTITIAADSIETAVKSELVNVAKKVRIDGFRKGKVPMNIVAQRYGASVRQDVLGDLMSRNFIDAIIKEKINPAGAPTYVPGEYKLGEDFTYSVEFEVYPEVELQGLEAIEVEKPIVEVTDADVDGMLDTLRKQQATWKEKDGAVEAEDRVTIDFTGSVDGEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKVEERELPELTAEFIKRFGVEDGSVEGLRAEVRKNMERELKSAIRNRVKSQAIEGLVKANDIDVPAALIDSEIDVLRRQAAQRFGGNEKQALELPRELFEEQAKRRVVVGLLLGEVIRTNELKADEERVKGLIEEMASAYEDPKEVIEFYSKNKELMDNMRNVALEEQAVEAVLAKAKVTEKETTFNELMNQQA
-
分子量
50.2 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
TIG recombinant proteins, derived from the TIG (trypsin inhibitor globulin) family, have garnered significant attention in biological and biomedical research due to their unique structural properties and versatile functional roles. These proteins are known for their ability to inhibit serine proteases, which play crucial roles in various physiological processes, including digestion, immune responses, and cell signaling. The investigation into TIG recombinant proteins has been motivated by their potential therapeutic applications, particularly in developing novel anti-inflammatory and anticancer agents. Advances in molecular cloning and protein expression technologies have enabled researchers to produce these proteins with enhanced purity and activity, facilitating the exploration of their molecular mechanisms and interaction with target proteases. Furthermore, studies have highlighted the potential of TIG proteins in modulating pathological conditions, thus opening avenues for innovative treatments. As a result, ongoing research is focused on characterizing the functional dynamics of TIG recombinant proteins, elucidating their roles in disease mechanisms, and leveraging their properties for drug development and therapeutic interventions.
