Analytical Data
-
基因名
SEPSECS
- Application
-
别名
SEPSECS;TRNP48;O-phosphoseryl-tRNA(Sec) selenium transferase
-
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
Q9HD40
-
表达区间
1-501aa
-
氨基酸序列
MGSSHHHHHH SSGLVPRGSH MNRESFAAGE RLVSPAYVRQ GCEARRSHEH LIRLLLEKGK CPENGWDEST LELFLHELAI MDSNNFLGNC GVGEREGRVA SALVARRHYR FIHGIGRSGD ISAVQPKAAG SSLLNKITNS LVLDIIKLAG VHTVANCFVV PMATGMSLTL CFLTLRHKRPKAKYIIWPRI DQKSCFKSMI TAGFEPVVIE NVLEGDELRT DLKAVEAKVQ ELGPDCILCI HSTTSCFAPR VPDRLEELAV ICANYDIPHIVNNAYGVQSS KCMHLIQQGA RVGRIDAFVQ SLDKNFMVPV GGAIIAGFND SFIQEISKMY PGRASASPSL DVLITLLSLG SNGYKKLLKE RKEMFSYLSN QIKKLSEAYN ERLLHTPHNP ISLAMTLKTL DEHRDKAVTQ GSMLFTRQV SGARVVPLGS MQTVSGYTFR GFMSHTNNYP CAYLNAASAI GMKMQDVDLF IKRLDRCLKA VRKERSKESD DNYDKTEDVD IEEMALKLDN VLLDTYQDAS S
-
分子量
58 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
SEPSECS (Selenocysteine Synthase) is a critical enzyme responsible for the incorporation of the 21st amino acid, selenocysteine, into proteins. This unique amino acid plays essential roles in various biological processes, including antioxidant defense and redox regulation, due to its presence in several important selenoproteins. The study of SEPSECS is particularly relevant in the context of human health and disease, as selenoproteins are implicated in cancer, cardiovascular diseases, and neurodegenerative disorders. Understanding the mechanisms of SEPSECS functioning and the regulation of selenocysteine incorporation can provide insights into the therapeutic potential of targeting selenoprotein pathways. Recent advances in recombinant protein technology have enabled the production of SEPSECS in various expression systems, facilitating the study of its structure and function. By investigating the molecular mechanisms underlying SEPSECS activity, researchers aim to elucidate its role in health and disease, paving the way for novel strategies in biomedical research and potential clinical applications. The exploration of SEPSECS and selenoproteins highlights the intricate relationship between nutrition, genetics, and disease, emphasizing the need for continued research in this field to harness the benefits of selenium in human health.
