Analytical Data
-
基因名
RNPEP
- Application
-
别名
RNPEP；APB；Aminopeptidase B
-
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
Q9H4A4
-
表达区间
1-650aa
-
氨基酸序列
MASGEHSPGSGAARRPLHSAQAVDVASASNFRAFELLHLHLDLRAEFGPP GPGAGSRGLSGTAVLDLRCLEPEGAAELRLDSHPCLEVTAAALRRERPGS EEPPAEPVSFYTQPFSHYGQALCVSFPQPCRAAERLQVLLTYRVGEGPGV CWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKYKYSALIEVPDG FTAVMSASTWEKRGPNKFFFQMCQPIPSYLIALAIGDLVSAEVGPRSRVW AEPCLIDAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGM ENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGF TMYAQRRISTILFGAAYTCLEAATGRALLRQHMDITGEENPLNKLRVKIE PGVDPDDTYNETPYEKGFCFVSYLAHLVGDQDQFDSFLKAYVHEFKFRSI LADDFLDFYLEYFPELKKKRVDIIPGFEFDRWLNTPGWPPYLPDLSPGDS LMKPAEELAQLWAAEELDMKAIEAVAISPWKTYQLVYFLDKILQKSPLPP GNVKKLGDTYPSISNARNAELRLRWGQIVLKNDHQEDFWKVKEFLHNQGK QKYTLPLYHAMMGGSEVAQTLAKETFASTASQLHSNVVNYVQQIVAPKGS
-
分子量
99 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
The research on RNPEP recombinant proteins has gained attention due to the significance of RNPEP (Arginine-N-glycyl Peptidase) in various physiological and pathological processes. RNPEP is an intracellular protease involved in the cleavage of arginine-glycine-rich peptides, playing a crucial role in protein homeostasis, cell signaling, and immune responses. Alterations in RNPEP activity have been implicated in several diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases. Understanding the structure and function of RNPEP can provide insights into its biological roles and potential therapeutic applications. The development of recombinant RNPEP proteins allows researchers to study the enzyme's mechanisms, substrate specificity, and interactions with other cellular proteins in a controlled environment. This knowledge is essential for exploring RNPEP as a target for drug development and for designing inhibitors that could modulate its activity in disease contexts. Additionally, the ability to produce these proteins in sufficient quantities opens avenues for further functional assays and structural studies, paving the way for advancing our understanding of RNPEP's contributions to health and disease.
