Analytical Data
-
Gene name
ADAM20
- Application
-
Alternative Names
Disintegrin and metalloproteinase domain-containing protein 20
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O43506
-
Expression Region
His367~Gly615
-
Molecular Weight
30kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
ADAM20, a member of the ADAM (A Disintegrin and Metalloproteinase) family, is characterized by its unique structure, comprising a metalloproteinase domain, a disintegrin-like domain, and a cysteine-rich domain, along with an ectodomain and a transmembrane region. Initially implicated in processes such as cell adhesion, migration, and proteolysis, ADAM20 has garnered significant attention in the context of various biological and pathological processes, including inflammation and cancer. Recent studies have highlighted its role in modulating immune responses and facilitating tumor progression, making it a candidate for therapeutic intervention. The recombinant production of ADAM20 protein allows for in-depth functional studies and the exploration of its enzymatic activity, shedding light on its mechanisms in cellular signaling and interaction with other proteins. Understanding the molecular dynamics and functional characteristics of ADAM20 is critical for developing targeted treatments in diseases where its expression and activity are dysregulated. Moreover, investigating ADAM20 may provide insights into its potential as a biomarker for certain cancers, enhancing early diagnosis and improving prognosis. Thus, research on recombinant ADAM20 protein is essential for clarifying its biological roles and therapeutic potentials.
