Mouse Tartrate Resistant Acid Phosphatase 5b ELISA kit
Specifications
| Product Cat#: | EK-07-0801 |
| Product name: | Mouse Tartrate Resistant Acid Phosphatase 5b ELISA kit |
| Target Name: | TRACP 5b |
| Species Reactivity: | Mouse |
| Product Size: | 48/96 Tests |
| Sensitivity: | 0.05 ng/ml |
| Assay range: | 2.5-50 ng/ml |
| Assay Time: | 90 minutes |
| Platform: | Colorimetric Microplate Reader |
| Conjugate: | HRP |
| ELISA Type: | Competitive ELISA |
| Detection Method: | Colorimetric |
| Storage temperature: | Store at 2-8°C |
| Stability: | Stable within the expiration date under suggested storage conditions |
| Shipping condition: | Wet ice |
| Kit Contents: | Microtiter plate (1x), Enzyme conjugate (1 vial), Standard samples (6 vials), |
| Substrates (A & B, 2 vials), Stop solution (1 vial), Wash Solution (100x, 1 vial), | |
| Balance solution (1 vial), Instruction (1 copy) | |
| Other Names of Target: | ACP5; HPAP; SPENCDI; TRAP |
Target information
Tartrate-resistant acid phosphatase (TRAP or TRAPase), also called acid phosphatase 5, tartrate resistant (ACP5), is a glycosylated monomeric metalloprotein enzyme expressed in mammals.It has a molecular weight of approximately 35kDa, a basic isoelectric point (7.6-9.5), and optimal activity in acidic conditions. TRAP is synthesized as latent proenzyme and activated by proteolytic cleavage and reduction.It is differentiated from other mammalian acid phosphatases by its resistance to inhibition by tartrate and molecular weight.The mechanism of phosphate ester hydrolysis by TRAP is through a nucleophilic attack mechanism,whereby, catalysis occurs with the binding of a phosphate-substrate to the Fe2+ in the active site of TRAP. This is then followed by a nucleophilic attack by a hydroxide ligand on the bound phosphorus atom, resulting in cleavage of the phosphate ester bond and production of an alcohol. The exact identity and mechanism of the hydroxide ligand is unclear, but it is thought to be either a hydroxide that bridges the metal ions within the active site or a terminal hydroxide bound to Fe3+, with conflicting reports for both mechanisms.
Provider
Erpantech Laboratory
