Analytical Data
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Gene name
DPYSL2
- Application
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Alternative Names
DPYSL2；CRMP2；ULIP2；Dihydropyrimidinase-related Protein 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16555
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Expression Region
1-572aa
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AA Sequence
MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFSLSGAQIDDNIPRRTTQRIVAPPGGRANITSLG
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Molecular Weight
64.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
Protein Description
The study of non-pathogenic chicken (NPC) recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including biotechnology, medicine, and agriculture. NPCs are considered an important source of proteins for research and industrial purposes, as they exhibit unique properties such as high stability, low immunogenicity, and the ability to elicit specific immune responses. The advent of recombinant DNA technology has enabled the production of NPC proteins in various host systems, enhancing efficiency and scalability while reducing the risk of contamination associated with traditional protein isolation methods. Researchers have been exploring the utility of NPC recombinant proteins in vaccine development, targeting specific pathogens, and improving livestock health. Additionally, the ability to engineer these proteins for enhanced functionality opens new avenues for developing therapeutic agents and diagnostic tools. The ongoing research focuses on optimizing expression systems, characterizing the functional properties of NPC recombinant proteins, and understanding their interactions in biological systems. The insights gained from this research are expected to contribute significantly to advancements in health and agricultural sciences, addressing challenges related to infectious diseases and improving animal production.
