Analytical Data
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Gene name
CELA3B
- Application
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Alternative Names
CELA3B；ELA3B；Chymotrypsin-like elastase family member 3B
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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
P08861
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Expression Region
29-270aa
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AA Sequence
VVNGEDAVPYSWPWQVSLQYEKSGSFYHTCGGSLIAPDWVVTAGHCISSSRTYQVVLGEYDRAVKEGPEQVIPINSGDLFVHPLWNRSCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQEALLPVVDYEHCSRWNWWGSSVKKTMVCAGGDIRSGCNGDSGGPLNCPTEDGGWQVHGVTSFVSAFGCNTRRKPTVFTRVSAFIDWIEETIASH
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Molecular Weight
30.0 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
CELA3B (Cathepsin E-Like Aspartic Protease 3B) is a member of the aspartic protease family, which is involved in various physiological and pathological processes, including protein degradation, immune response, and tissue remodeling. Research on CELA3B has gained significance due to its potential role in cancer progression, inflammation, and neurodegenerative diseases. Preliminary studies have suggested that CELA3B may contribute to tumor microenvironment remodeling and influence the behavior of cancer cells. As a result, understanding its activity and regulation is crucial for elucidating its biological functions and implications in disease. Recombination techniques have enabled researchers to produce CELA3B in a controlled environment, facilitating the investigation of its enzymatic properties and interactions with substrate proteins. This not only aids in defining its functional role but also paves the way for potential therapeutic strategies targeting CELA3B in various diseases. Additionally, insights into its structure-function relationships could lead to the development of selective inhibitors, offering a promising avenue for drug discovery. Overall, the study of CELA3B recombinant proteins serves as a vital link in understanding the broader implications of aspartic proteases in human health and disease.
