Analytical Data
-
Gene name
ADAM11
- Application
-
Alternative Names
ADAM11; MDC; Disintegrin and metalloProteinase domain-containing Protein 11
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O75078
-
Expression Region
25-93aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMGPYGANMEDSVCCRDYVRYRLPLRVVKHFYWTSDSCPRPGVVLLTFRDKEICADPRVPWVKMILNKLSQ
-
Molecular Weight
10.3 KDa
-
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
ADAM11 (A Disintegrin and Metalloproteinase 11) is a member of the ADAM family of proteins, which are characterized by their disintegrin and metalloproteinase domains. These proteins play crucial roles in various biological processes, including cell adhesion, migration, and proteolytic cleavage of extracellular matrix components. Research has indicated that ADAM11 is implicated in key physiological and pathological processes, including neurogenesis, synaptic plasticity, and certain cancers. The significance of ADAM11 in human health has prompted investigations into its structure and function, particularly its role in cell signaling pathways. Recombination technologies have enabled the production of recombinant ADAM11 protein, facilitating detailed studies of its activity, interactions with other proteins, and potential therapeutic applications. Understanding the biochemical properties of this protein at the molecular level could illuminate its function in normal biology as well as its role in disease progression. Moreover, recombinant ADAM11 could serve as a valuable tool for drug development and biomarker identification in disease contexts, particularly in neurological and oncological research. Overall, the study of recombinant ADAM11 is pivotal for advancing our comprehension of its biological roles and therapeutic potential.
