Analytical Data
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基因名
Marapsin/Pancreasin
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简介
Marapsin/pancreatin protein shows predominant expression in the pancreas, emphasizing its central role in pancreatic tissue. As a key member within this organ, marapsin/pancreatin may play a crucial role in pancreatic function and processes. Marapsin/Pancreasin Protein, Human (HEK293, His) is the recombinant human-derived Marapsin/Pancreasin protein, expressed by HEK293 , with C-His labeled tag.
- Application
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别名
Serine protease 27; Marapsin; Pancreasin; PRSS27; MPN
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种属
Human
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表达系统
HEK293
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标签
C-6*His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9BQR3
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表达区间
A23-K290
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氨基酸序列
ATACGRPRMLNRMVGGQDTQEGEWPWQVSIQRNGSHFCGGSLIAEQWVLTAAHCFRNTSETSLYQVLLGARQLVQPGPHAMYARVRQVESNPLYQGTASSADVALVELEAPVPFTNYILPVCLPDPSVIFETGMNCWVTGWGSPSEEDLLPEPRILQKLAVPIIDTPKCNLLYSKDTEFGYQPKTIKNDMLCAGFEEGKKDACKGDSGGPLVCLVGQSWLQAGVISWGEGCARQNRPGVYIRVTAHHNWIHRIIPKLQFQPARLGGQK
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蛋白长度
Full Length of Mature Protein
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分子量
35-45 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
Marapsin and Pancreasin are recombinant proteins that have garnered significant interest due to their potential therapeutic applications. Marapsin, originally identified in the venom of the South American snake Bothrops asper, is a serine protease known for its ability to cleave specific peptide bonds, which may have implications for understanding protein interactions and developing novel therapeutic agents. On the other hand, Pancreasin, a mixture of digestive enzymes derived from the porcine pancreas, serves as a critical component for addressing pancreatic insufficiency in patients, aiding in the digestion and absorption of nutrients. The recombinant production of these proteins not only facilitates a consistent supply but also allows for the modification of their properties to enhance functionality and efficacy. Research into their structure-function relationships has led to insights into their mechanisms of action, paving the way for optimized enzyme formulations. Furthermore, advances in recombinant DNA technology have enabled the exploration of these proteins in various biomedical contexts, including drug delivery systems and enzyme replacement therapies. The ongoing investigation into Marapsin and Pancreasin highlights the broader significance of recombinant proteins in modern medicine, focusing on the need for innovative treatments for metabolic disorders and other health challenges. By harnessing the unique properties of these enzymes, researchers aim to improve therapeutic strategies and enhance the quality of life for individuals affected by digestive and metabolic deficiencies.












