Analytical Data
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Gene name
ADAM8
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简介
The ADAM10 protein cleaves TNF-α precursor, releasing a soluble form, and mediates the proteolytic release of JAM3 and various cell surface proteins. ADAM10 Protein, Human (HEK293, His) is the recombinant human-derived ADAM10 protein, expressed by HEK293 , with C-10*His labeled tag.
- Application
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Species
Human
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Source
HEK293
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Tag
C-10*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
O14672
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Expression Region
T214-E672
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Protein Length
Extracellular Domain (with Propeptide)
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Molecular Weight
60-71 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
ADAM8, a member of the ADAM (A Disintegrin and Metalloproteinase) family, is a type I transmembrane protein characterized by its structure that includes a pro-domain, a metalloproteinase domain, a disintegrin domain, a cysteine-rich domain, and an epidermal growth factor-like domain. Research has highlighted ADAM8's significant role in various biological processes, including cell adhesion, migration, and signaling, particularly in the context of inflammation, cancer progression, and tissue remodeling. Elevated levels of ADAM8 have been associated with several pathological conditions, such as asthma, rheumatoid arthritis, and tumors, where it contributes to the cleavage of various substrates, affecting the tumor microenvironment and immune responses. The ability of ADAM8 to modulate these processes makes it a potential therapeutic target, warranting its recombinant protein production for studying its function and the underlying mechanisms involved. By utilizing recombinant DNA technology, researchers aim to produce ADAM8 in a controlled environment, enabling detailed analysis of its enzymatic activity, binding capabilities, and its interactions with other cellular components. This research not only elucidates the role of ADAM8 in health and disease but also paves the way for developing targeted inhibitors that could provide novel treatment options for ADAM8-related disorders. Understanding the structure-function relationship of ADAM8 through recombinant studies may lead to significant advancements in medical research, particularly in the fields of oncology and immunology.
