Recombinant Human AOC3 (C-Fc)
- Cat. No.：EPT235
- Price：Negotiable
- Clicks：1560
Product Detail
Basic Information
| Size | 10ug |
|---|
| Expression Host | Human Cells |
|---|
| Tag | C-Fc |
|---|
Physical Properties
| Molecular Weight | 108.5 KDa |
|---|
| Apparent Molecular Weight | 120 KDa, reducing conditions |
|---|
| Form | Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 500mM NaCl, pH 8.0. |
|---|
| Purity | Greater than 95% as determined by reducing SDS-PAGE. |
|---|
Activity & Endotoxin
| Endotoxin Level | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
|---|
Storage & Shipping
| Reconstitution | Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
|---|
| Storage | Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
|---|
| Shipping Condition | The product is shipped at ambient temperature.
Upon receipt, store it immediately at the temperature listed below. |
|---|
Detailed Description
| Background | Membrane primary amine oxidase(AOC3), also known as vascular adhesion protein (VAP-1) and HPAO, this protein is a member of the semicarbazide-sensitive amine oxidase (SSAO) family. VAP-1 is a type 1 membrane-bound glycoprotein that has a distal adhesion domain and an enzymatically active amine oxidase site outside of the membrane, VAP-1 has adhesive properties, functional monoamine oxidase activity, and possibly plays a role in glucose handling, leukocyte trafficking, and migration during inflammation. This rise in metabolic products contributes to generating advanced glycation end-products and oxidative stress along with the monoamine detoxification in the organism. It is highly expressed on the endothelium of the lung and trachea, and absent from leukocytes and epithelial cells. Membrane-bound VAP-1 releases an active, soluble form of the protein, which may be conducive to increased inflammation and the progression of many vascular disorders. In particular, elevation of VAP-1 activity and the increased enzymatic-mediated deamination is proposed to play a role in renal and vascular disease, oxidative stress, acute and chronic hyperglycemia, and diabetes complications. |
|---|
