关键信息
-
基因名
ERp57
- 应用
-
别名
ERp57；ERP57；ERP60；GRP58；Protein disulfide-isomerase A3
-
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
P30101
-
表达区间
25-505aa
-
氨基酸序列
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMSDV LELTDDNFES RISDTGSAGL MLVEFFAPWC GHCKRLAPEY EAAATRLKGI VPLAKVDCTA NTNTCNKYGV SGYPTLKIFR DGEEAGAYDG PRTADGIVSH LKKQAGPASV PLRTEEEFKK FISDKDASIV GFFDDSFSEA HSEFLKAASN LRDNYRFAHT NVESLVNEYD DNGEGIILFR PSHLTNKFED KTVAYTEQKM TSGKIKKFIQ ENIFGICPHM TEDNKDLIQG KDLLIAYYDV DYEKNAKGSN YWRNRVMMVA KKFLDAGHKL NFAVASRKTF SHELSDFGLE STAGEIPVVA IRTAKGEKFV MQEEFSRDGK ALERFLQDYF DGNLKRYLKS EPIPESNDGP VKVVVAENFD EIVNNENKDV LIEFYAPWCG HCKNLEPKYK ELGEKLSKDP NIVIAKMDAT ANDVPSPYEV RGFPTIYFSP ANKKLNPKKY EGGRELSDFI SYLQREATNP PVIQEEKPKK KKKAQEDL
-
分子量
59 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.
质检流程
相关产品
背景信息
ERp57, also known as endoplasmic reticulum protein 57, is a critical member of the protein disulfide isomerase (PDI) family, primarily involved in the formation and rearrangement of disulfide bonds in nascent glycoproteins within the endoplasmic reticulum. This enzyme plays a pivotal role in protein folding, quality control, and the overall maturation of proteins that are essential for various physiological processes. Studies have highlighted ERp57's involvement in immune responses and its interaction with various chaperones, which influences both protein stability and functionality. Research has also suggested that dysregulation of ERp57 can lead to various diseases, including neurodegenerative disorders and cancers. Therefore, the understanding of ERp57's mechanisms and its interactions has garnered significant interest in the fields of cell biology and molecular medicine. As a potential therapeutic target, recombinant ERp57 has been studied for its capability to improve protein folding and stability, which opens avenues for biotechnological applications in developing biopharmaceuticals. The exploration of ERp57's structure-function relationship through recombinant protein techniques aims to shed light on its role in cellular processes and therapeutic potential, highlighting the importance of this enzyme in both fundamental research and practical applications in disease treatment and biotechnology.
