ACPP antibody from Promab.
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A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. ACP3 has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.
For research use only.
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
| Species | WB | IHC | IHC-P | IHC-F | IF/ICC | Flow Cytometry | ELISA | IP | ChIP |
|---|---|---|---|---|---|---|---|---|---|
| Human | |||||||||
| Mouse | |||||||||
| Rat |
This product is manufactured by Promab and sold through ABMIUM without relabelling.
ABMIUM supports global orders. Availability, shipping requirements and applicable import arrangements are confirmed before fulfilment where required.
Yes. Send your target, sample, application and experimental conditions through ABMIUM MATCH or technical support.
Unless the listing expressly states otherwise, ABMIUM products are supplied for research use only and are not for diagnostic or therapeutic use.
Acid phosphatase 3 (ACP3), better known as prostatic acid phosphatase (PAP or ACPP), is a human phosphatase classically associated with prostate tissue and acidic phosphomonoester hydrolysis.
Biological function: ACP3/prostatic acid phosphatase is a histidine acid phosphatase that hydrolyses phosphate monoesters under acidic conditions and can dephosphorylate phosphorylated substrates. Alternative forms of the protein include secreted and membrane-associated isoforms, supporting research into extracellular phosphatase and nucleotide-metabolism biology.
