Analytical Data
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Gene name
ADAM12
- Application
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Alternative Names
ADAM12；MLTN；Disintegrin and metalloProteinase domain-containing Protein 12
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Species
Mouse
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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
Q61824
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Expression Region
206-706aa
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AA Sequence
ETLKMTKYVELVIVADNREFQRQGKDLEKVKQRLIEIANHVDKFYRPLNI RIVLVGVEVWNDIDKCSISQDPFTSLHEFLDWRKIKLLPRKSHDNAQLIS GVYFQGTTIGMAPIMSMCTAEQSGGVVMDHSDSPLGAAVTLAHELGHNFG MNHDTLERGCSCRMAAEKGGCIMNPSTGFPFPMVFSSCSRKDLEASLEKG MGMCLFNLPEVKQAFGGRKCGNGYVEEGEECDCGEPEECTNRCCNATTCT LKPDAVCAHGQCCEDCQLKPPGTACRGSSNSCDLPEFCTGTAPHCPANVY LHDGHPCQGVDGYCYNGICQTHEQQCVTLWGPGAKPAPGICFERVNSAGD PYGNCGKDSKSAFAKCELRDAKCGKIQCQGGASRPVIGTNAVSIETNIPQ QEGGRILCRGTHVYLGDDMPDPGLVLAGTKCAEGKICLNRRCQNISVFGV HKCAMQCHGRGVCNNRKNCHCEAHWAPPFCDKFGFGGSTDSGPIRQADNQ G
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Molecular Weight
58 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
ADAM12 (A Disintegrin and Metalloproteinase 12) is a member of the ADAM family, which is characterized by its disintegrin and metalloproteinase domains. It plays a crucial role in various biological processes, including cell adhesion, motility, and proteolytic cleavage of substrates, which are essential for development and tissue remodeling. Research has indicated that ADAM12 is involved in pathological conditions such as cancer progression, inflammation, and cardiovascular diseases. Its expression levels can serve as potential biomarkers for certain cancers, making it an attractive target for therapeutic intervention. The recombinant expression of ADAM12 has generated significant interest, as it enables the study of its functional domains and interactions with other proteins. By producing ADAM12 in a recombinant form, researchers can investigate its enzymatic activity, inhibition mechanisms, and interactions with various substrates, providing insights into its role in disease processes. Furthermore, understanding ADAM12's structure-function relationship could lead to the development of specific inhibitors that may have therapeutic implications in cancer therapy and other diseases associated with dysregulated ADAM12 activity. Thus, the investigation of recombinant ADAM12 is not only vital for elucidating its biological functions but also for exploring its potential as a therapeutic target.
