Analytical Data
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Gene name
ADAM10
- Application
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Alternative Names
ADAM10；KUZ；MADM；Disintegrin and metalloProteinase domain-containing Protein 10
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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
O14672
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Expression Region
214 -672aa
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AA Sequence
TSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMDPSTCASTGSVQWSRHFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAE
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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
ADAM10 (A Disintegrin and metalloproteinase 10) is a member of the ADAM family of proteins that play critical roles in various biological processes, including cell adhesion, migration, and proteolytic processing of membrane proteins. This enzyme is particularly important in the context of neurobiology and cancer research, as it is involved in the shedding of essential molecules such as the amyloid precursor protein (APP) and Notch ligands, influencing both neurodegenerative diseases and cellular signaling pathways. The study of recombinant ADAM10 protein seeks to elucidate its structure-function relationships, enzymatic activity, and regulatory mechanisms. By producing ADAM10 in a recombinant form, researchers can investigate its interactions with substrates and inhibitors, which can lead to the identification of potential therapeutic targets for diseases where ADAM10 activity is dysregulated. Additionally, understanding ADAM10's role in cell biology contributes to a deeper comprehension of its implications in tumorigenesis and neural development. As such, the ongoing research into recombinant ADAM10 not only aims to clarify its functional attributes but also to explore its potential as a biomarker or therapeutic intervention in diseases characterized by aberrant proteolytic activity.
