Analytical Data
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基因名
RNPEPL1
- Application
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别名
RNPEPL1; Aminopeptidase RNPEPL1; EC 3.4.11.-; Arginyl aminopeptidase-like 1; Methionyl aminopeptidase; EC 3.4.11.18
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9HAU8
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表达区间
1-494 aa
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氨基酸序列
MSATRSAYME EEGVFHFHME HPVPAYLVAL VAGDLKPADI GPRSRVWAEP CLLPTATSKL SGAVEQWLSA AERLYGPYMW GRYDIVFLPP SFPIVAMENP CLTFIISSIL ESDEFLVIDV IHEVAHSWFG NAVTNATWEE MWLSEGLATY AQRRITTETY GAAFTCLETA FRLDALHRQM KLLGEDSPVS KLQVKLEPGV NPSHLMNLFT YEKGYCFVYY LSQLCGDPQR FDDFLRAYVE KYKFTSVVAQ DLLDSFLSFF PELKEQSVDC RAGLEFERWL NATGPPLAEP DLSQGSSLTR PVEALFQLWT AEPLDQAAAS ASAIDISKWR TFQTALFLDR LLDGSPLPQE VVMSLSKCYS SLLDSMNAEI RIRWLQIVVR NDYYPDLHRV RRFLESQMSR MYTIPLYEDL CTGALKSFAL EVFYQTQGRL HPNLRRAIQQ ILSQGLGSST EPASEPSTEL GKAEADTDSD AQALLLGDEA PSSAISLRDV NVSA
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分子量
80.0 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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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
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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.
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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.
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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
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Protein Description
RNPEPL1, also known as Ribonuclease P Protein Subunit 1, is a crucial component of the ribonuclease P complex, which plays an essential role in tRNA processing by cleaving precursor tRNA molecules to generate mature tRNAs. This protein has garnered significant attention in recent years due to its involvement in various cellular processes and potential implications in diseases. Research has indicated that RNPEPL1 may influence pathways related to cancer progression and neurodegenerative disorders, highlighting its importance in cellular homeostasis and gene regulation. The understanding of RNPEPL1's structure and function remains limited, prompting scientists to investigate its biochemical properties, interactions with other proteins, and regulatory mechanisms. Furthermore, the development of recombinant RNPEPL1 proteins has opened new avenues for studying its functional roles in vitro and in vivo, providing insights into its contribution to cellular metabolism and potential therapeutic targets. This growing body of research aims to unravel the complexities of RNPEPL1, paving the way for novel strategies in disease treatment and a deeper understanding of fundamental biological processes.
