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ZMPSTE24 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O75844 |
|---|---|
| Other Accession | NP_005848 |
| Clone Names | 3092508 |
| Gene ID | 10269 |
|---|---|
| Other Names | CAAX prenyl protease 1 homolog, Farnesylated proteins-converting enzyme 1, FACE-1, Prenyl protein-specific endoprotease 1, Zinc metalloproteinase Ste24 homolog, ZMPSTE24, FACE1, STE24 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2415b was selected from the C-term region of human ZMPSTE24 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | ZMPSTE24 |
|---|---|
| Synonyms | FACE1, STE24 |
| Function | Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C. |
| Cellular Location | Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus inner membrane; Multi-pass membrane protein |
| Tissue Location | Widely expressed. High levels in kidney, prostate, testis and ovary |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
ZMPSTE24 is a zinc metalloprotease similar to yeast Ste24p. It is an integral membrane protein belonging to peptidase family M48 and is found in the endoplasmic reticulum and possibly in the Golgi compartment. It is thought to be involved in the proteolytic processing of farnesylated proteins.
References
Freije, J.M., et al., Genomics 58(3):270-280 (1999).Kumagai, H., et al., Biochim. Biophys. Acta 1426(3):468-474 (1999).Tam, A., et al., J. Cell Biol. 142(3):635-649 (1998).
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