Analytical Data
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Gene name
alp2
- Application
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Alternative Names
alp2；Alkaline protease 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
P87184
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Expression Region
137-495aa
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AA Sequence
EDPTVEKSAPWGLARISHRDSLSFGTFNKYLYASEGGEGVDAYTIDTGINVDHVDFEGRAQWGKTIPTDDEDADGNGHGTHCSGTIAGRKYGVAKKANLYAVKVLRSSGSGTMSDVVAGVEWAVKSHLKKVKDAKDGKIKGFKGSVANMSLGGGKSRTLEAAVNAGVEAGLHFAVAAGNDNADACNYSPAAAENPITVGASTLQDERAYFSNYGKCTDIFAPGLNILSTWIGSKHAVNTISGTSMASPHIAGLLAYFVSLQPSKDSAFAVDELTPKKLKKDIIAIATQGALTDIPSDTPNLLAWNGGGSSNYTDIIASGGYKVNASVKDRFEGLVHKAEKLLTEELGAIYSEIHDAAVA
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Molecular Weight
45.0 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 the Alp2 recombinant protein is grounded in its significance in various biological processes and potential applications in biotechnology and medicine. Alp2, a protein derived from fungal or bacterial sources, has been implicated in microbial interactions, particularly in host-pathogen dynamics. Understanding the molecular structure and function of Alp2 is crucial for elucidating its role in virulence, which can inform the development of novel therapeutic strategies against infectious diseases. Additionally, recombinant technology allows for the production of purified Alp2 in vitro, enabling detailed characterization studies. This research is particularly relevant in the context of rising antibiotic resistance, where alternative approaches to infection control are urgently needed. Furthermore, leveraging Alp2's properties could contribute to advancements in vaccine development, as it may serve as a potential antigen or adjuvant. As researchers continue to explore the functionality of Alp2, insights gleaned from such studies could pave the way for innovative solutions in healthcare and beyond, thereby reflecting the broader significance of recombinant protein research in contemporary science.
