Analytical Data
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Gene name
ADAM1
- Application
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Alternative Names
FTNAP; PH-30a; Ftna; ADAM1P; Fertilin Alpha; Disintegrin and metalloproteinase domain-containing protein 1
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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
P70505
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Expression Region
Ser463~Gly727
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Molecular Weight
37kDa
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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
ADAM1 (A Disintegrin and Metalloproteinase 1) is a member of the ADAM family, which plays a pivotal role in various biological processes, including cell adhesion, migration, and shedding of substrate proteins. Initially identified for its involvement in fertilization as a sperm-specific protein that facilitates oocyte interaction, ADAM1 has garnered attention for its potential implications in reproductive biology and beyond. Research has highlighted its role in modulating signaling pathways and influencing extracellular matrix dynamics, which are crucial in development and disease progression. Various studies suggest that ADAM1 may contribute to pathological conditions such as cancer metastasis and tissue remodeling. The recombinant expression of ADAM1 protein is vital for elucidating its structure-function relationships, investigating its enzymatic activities, and understanding its interaction with other molecules. Moreover, ADAM1's distinct domains, including its metalloproteinase and disintegrin domains, present opportunities for targeted therapeutic interventions. Advances in protein engineering and expression systems have enabled the production of high-quality recombinant ADAM1, facilitating in vitro and in vivo studies. As a result, ongoing research focuses on characterizing ADAM1's molecular functions and exploring its potential as a biomarker or therapeutic target in various diseases, thereby cementing its significance in both fundamental biology and clinical applications.











