Analytical Data
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基因名
THOP1
- Application
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别名
THOP1；Thimet oligopeptidase
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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
P52888
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表达区间
2-689aa
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氨基酸序列
KPPAACAGDMADAASPCSVVNDLRWDLSAQQIEERTRELIEQTKRVYDQV GTQEFEDVSYESTLKALADVEVTYTVQRNILDFPQHVSPSKDIRTASTEA DKKLSEFDVEMSMREDVYQRIVWLQEKVQKDSLRPEAARYLERLIKLGRR NGLHLPRETQENIKRIKKKLSLLCIDFNKNLNEDTTFLPFTLQELGGLPE DFLNSLEKMEDGKLKVTLKYPHYFPLLKKCHVPETRRKVEEAFNCRCKEE NCAILKELVTLRAQKSRLLGFHTHADYVLEMNMAKTSQTVATFLDELAQK LKPLGEQERAVILELKRAECERRGLPFDGRIRAWDMRYYMNQVEETRYCV DQNLLKEYFPVQVVTHGLLGIYQELLGLAFHHEEGASAWHEDVRLYTARD AASGEVVGKFYLDLYPREGKYGHAACFGLQPGCLRQDGSRQIAIAAMVAN FTKPTADAPSLLQHDEVETYFHEFGHVMHQLCSQAEFAMFSGTHVERDFV EAPSQMLENWVWEQEPLLRMSRHYRTGSAVPRELLEKLIESRQANTGLFN LRQIVLAKVDQALHTQTDADPAEEYARLCQEILGVPATPGTNMPATFGHL AGGYDAQYYGYLWSEVYSMDMFHTRFKQEGVLNSKVGMDYRSCILRPGGS EDASAMLRRFLGRDPKQDAFLLSKGLQVGGCEPEPQVC
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分子量
79 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
THOP1 (Thimet Oligopeptidase 1) is a metallopeptidase that plays a crucial role in the degradation of bioactive peptides, influencing various physiological processes, including neuropeptide metabolism and immune responses. Characterized by its ability to cleave peptide bonds at the N-terminus of short peptides, THOP1 is involved in the regulation of neuropeptides that affect pain, mood, and stress responses, making it a target of interest in studying neurodegenerative diseases and psychological disorders. Research has highlighted its potential implications in cancer biology, as altered THOP1 expression levels can affect tumor growth and metastasis through modulation of peptide signaling pathways. Despite its significance, the structural and functional characterizations of THOP1 remain limited. Recent advances in recombinant protein technology provide opportunities to produce and purify THOP1 for in-depth studies. The generation of recombinant THOP1 enables researchers to investigate its enzymatic activity, substrate specificity, and regulatory mechanisms, which could uncover potential therapeutic targets for diseases linked to THOP1 dysregulation. As understanding the biochemical properties of THOP1 can aid in elucidating its precise role in cellular processes, ongoing studies are anticipated to enhance our comprehension of its function in health and disease.
