Analytical Data
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基因名
XPNPEP1
- Application
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别名
XPNPEP1；XPNPEPL；Xaa-Pro aminopeptidase 1
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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
Q9NQW7
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表达区间
2-623aa
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氨基酸序列
PPKVTSELLRQLRQAMRNSEYVTEPIQAYIIPSGDAHQSEYIAPCDCRRA FVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDSNWTLMKMGLKDTP TQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLIPVKENLV DKIWTDRPERPCKPLLTLGLDYTGISWKDKVADLRLKMAERNVMWFVVTA LDEIAWLFNLRGSDVEHNPVFFSYAIIGLETIMLFIDGDRIDAPSVKEHL LLDLGLEAEYRIQVHPYKSILSELKALCADLSPREKVWVSDKASYAVSET IPKDHRCCMPYTPICIAKAVKNSAESEGMRRAHIKDAVALCELFNWLEKE VPKGGVTEISAADKAEEFRRQQADFVDLSFPTISSTGPNGAIIHYAPVPE TNRTLSLDEVYLIDSGAQYKDGTTDVTRTMHFGTPTAYEKECFTYVLKGH IAVSAAVFPTGTKGHLLDSFARSALWDSGLDYLHGTGHGVGSFLNVHEGP CGISYKTFSDEPLEAGMIVTDEPGYYEDGAFGIRIENVVLVVPVKTKYNF NNRGSLTFEPLTLVPIQTKMIDVDSLTDKECDWLNNYHLTCRDVIGKELQ KQGRQEALEWLIRETQPISKQH
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分子量
70 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
XPNPEP1, also known as the X-prolyl aminopeptidase 1, is a metallopeptidase that plays a critical role in the processing of bioactive peptides and proteins. This enzyme specifically cleaves N-terminal proline residues from polypeptides, which is essential for various physiological processes, including immune response, tissue regeneration, and metabolic regulation. Research has revealed that XPNPEP1 is implicated in several pathophysiological conditions, including cancer, neurodegenerative disorders, and cardiovascular diseases, highlighting its potential as a therapeutic target. The recombinant expression of XPNPEP1 enables comprehensive studies of its enzymatic activity, structure-function relationships, and interactions with substrates and inhibitors. Understanding the molecular mechanisms underlying XPNPEP1's function could lead to the development of novel therapeutic strategies for diseases associated with its dysregulation. Additionally, recombinant XPNPEP1 can be utilized in various biotechnological applications, including peptide engineering and drug development. Overall, the investigation of XPNPEP1 at the protein level holds significant promise for advancing our knowledge of peptide metabolism and providing insights into disease mechanisms.
