Analytical Data
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基因名
Serpina3n
- Application
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别名
Serpina3n；Spi2；Serine protease inhibitor A3N
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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
P29508
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表达区间
1-390aa
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氨基酸序列
MGSSHHHHHHSSGLVPRGSHMGSMNSLSEANTKFMFDLFQQFRKSKENNI FYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKAATYHVDR SGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFY QTSESVDFANAPEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLNA IYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQA KVLEIPYKGKDLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETR VDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSRGLVLSGVL HKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEEFHCNHPFLFFIRQNKTN SILFYGRFSSP
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分子量
47 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
Serpina3n, a member of the serine proteinase inhibitors (serpins) family, has garnered significant attention in biomedical research due to its potential roles in various physiological and pathological processes. Originally identified for its involvement in the regulation of inflammation and immune responses, Serpina3n has been linked to multiple diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Its ability to inhibit serine proteases implies a crucial function in maintaining homeostasis within the extracellular environment. Researchers are particularly interested in understanding the structural and functional properties of recombinant Serpina3n, as these insights could lead to the development of novel therapeutic strategies. Recombinant protein expression systems allow for the production of Serpina3n in a controlled manner, enabling detailed studies on its activity, interaction with target proteases, and potential applications in drug design. By elucidating the mechanisms through which Serpina3n exerts its effects, scientists hope to uncover new biomarkers for disease progression and develop targeted interventions that leverage its inhibitory functions. This research is further supported by advances in proteomics and structural biology, which facilitate the exploration of Serpina3n's complex interactions and regulatory networks within the body. Overall, the study of Serpina3n as a recombinant protein offers promising avenues for enhancing our understanding of its biological significance and therapeutic potential.
