Analytical Data
-
基因名
pepP
- Application
-
别名
pepP；PEPP2；THG1；Rhox homeobox family member 2
-
种属
E.coli
-
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
P15034
-
表达区间
2-441aa
-
氨基酸序列
SEISRQEFQ RRRQALVEQM QPGSAALIFA APEVTRSADS EYPYRQNSDF WYFTGFNEPE AVLVLIKSDD THNHSVLFNR VRDLTAEIWF GRRLGQDAAP EKLGVDRALA FSEINQQLYQ LLNGLDVVYH AQGEYAYADV IVNSALEKLR KGSRQNLTAP ATMIDWRPVV HEMRLFKSPE EIAVLRRAGE ITAMAHTRAM EKCRPGMFEY HLEGEIHHEF NRHGARYPSY NTIVGSGENG CILHYTENEC EMRDGDLVLI DAGCEYKGYA GDITRTFPVN GKFTQAQREI YDIVLESLET SLRLYRPGTS ILEVTGEVVR IMVSGLVKLG ILKGDVDELI AQNAHRPFFM HGLSHWLGLD VHDVGVYGQD RSRILEPGMV LTVEPGLYIA PDAEVPEQYR GIGIRIEDDI VITETGNENL TASVVKKPEE IEALMVAARK Q
-
分子量
49.8 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
Recombinant E.coli ystB Protein，His
Cat：PA2000-2341
Recombinant Human C1QDC1 Protein，GST
Cat：PA2000-6149
Protein Description
PepP, or peptidase P, is an important enzyme that plays a crucial role in various biological processes, including protein metabolism and regulation. Studying pepP recombinant proteins is vital for several reasons. First, the elucidation of its structure and function can provide insights into the enzymatic mechanisms of peptide cleavage, which is fundamental for understanding protein turnover and amino acid availability in cells. Furthermore, investigating pepP has implications in medicine, particularly in the context of various diseases where peptide regulation is disrupted, such as cancer and metabolic disorders. Recombinant techniques allow for the production of large quantities of pure pepP proteins, facilitating detailed biochemical assays, structural analyses, and potential therapeutic applications. Moreover, the alignment of pepP from various organisms aids in the comparative study of evolutionary adaptations in peptide metabolism. The production of recombinant pepP can also support the development of inhibitors or modulators that could serve as valuable tools in both research and therapeutic settings. Overall, the study of pepP recombinant proteins is a multidisciplinary endeavor that bridges biochemistry, molecular biology, and pharmacology, with the potential to advance our understanding of fundamental biological processes and to drive innovations in disease treatment.
