Analytical Data
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Gene name
ADAM5
- Application
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Alternative Names
tMDCII; TMDC2; Putative transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein II; Disintegrin and metalloproteinase domain-containing protein 5
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5BK84
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Expression Region
Cys413~Gln649
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Molecular Weight
30kDa
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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
ADAM5 (A Disintegrin and Metalloproteinase 5) is a member of the ADAM family, known for its role in various biological processes such as cell adhesion, migration, and proteolytic processing of membrane proteins. It consists of a disintegrin domain, a metalloproteinase domain, and a cysteine-rich domain, allowing it to interact with multiple substrates and modulate cell signaling pathways. The research into ADAM5 has gained traction due to its involvement in key physiological and pathological processes, including neurodevelopment, inflammation, and cancer progression. Notably, ADAM5 has been implicated in the shedding of neurotrophins and adhesion molecules, which are critical in neuronal function and signaling. Furthermore, dysregulation of ADAM5 activity has been linked to several diseases, suggesting its potential as a biomarker and therapeutic target. Protein engineering techniques to produce recombinant ADAM5 have facilitated in-depth studies on its structure-function relationships, enzymatic properties, and interactions with inhibitors or substrates. These advancements aim to elucidate the functional role of ADAM5 in health and disease, making it a promising candidate for drug development. The continuous investigation of ADAM5 could ultimately lead to a better understanding of its biological significance and therapeutic implications and provide insights into the development of novel treatments for conditions influenced by this enzyme. As research progresses, recombinant ADAM5 protein remains a valuable tool for characterizing the enzyme’s function and exploring its potential applications in biomedical science.
