Analytical Data
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Gene name
SPN
- Application
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Alternative Names
SPN；RNUT1；SPN1；Snurportin-1
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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
P16150
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Expression Region
20-253aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSSTTAVQT PTSGEPLVST SEPLSSKMYT TSITSDPKAD STGDQTSALP PSTSINEGSP LWTSIGASTG SPLPEPTTYQ EVSIKMSSVP QETPHATSHP AVPITANSLG SHTVTGGTIT TNSPETSSRT SGAPVTTAAS SLETSRGTSG PPLTMATVSL ETSKGTSGPP VTMATDSLET STGTTGPPVT MTTGSLEPSS GASGPQVSSV KLSTMMSPTT STNASTVPFR NPDENSR
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Molecular Weight
26 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 SPN (Serratia plymuthica nep1) recombinant proteins has gained significant attention in recent years due to their potential applications in various fields, including biotechnology and medicine. SPN proteins, particularly those involved in pathogenic interactions, have been shown to possess unique properties that can be harnessed for therapeutic purposes. For instance, the SPN proteins may play a crucial role in plant-pathogen interactions, offering insights into disease resistance mechanisms in crops. This research background highlights the importance of understanding the structure and function of these proteins, which can aid in the development of innovative strategies for disease management and crop protection. Furthermore, the ability to produce recombinant SPN proteins paves the way for exploring their biochemical properties and potential utilization in drug development, such as antimicrobial agents or biocontrol agents in agriculture. The ongoing research efforts are focused on elucidating the molecular mechanisms underlying the action of SPN proteins and their interactions with host organisms, thereby contributing to a deeper understanding of their biological significance and practical applications.
