Human Cathepsin X/Z/P Biotinylated Antibody Summary
Ala21-Val303 (Gly23Val, Ser48Thr)
Accession # Q9UBR2
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Cathepsin X/Z/P in Human Breast Cancer Tissue. Cathepsin X/Z/P was detected in immersion fixed paraffin-embedded sections of human breast cancer tissue using Goat Anti-Human Cathepsin X/Z/P Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF934) at 3 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (CTS013). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm. Staining was performed using our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Cathepsin X/Z/P
Cathepsin X (also known as Cathepsin Z and P) is a cysteine protease of the papain family (1‑5). Compared to other members of the papain family, Cathepsin X has a short proregion and unique insertions. The cysteine residue in the proregion forms a covalent and reversible bond with the active site cysteine residue (6). Acting as a carboxypeptidase, Cathepsin X displays a unique specificity (7‑10). It is ubiquitously expressed in human tissues and conserved in other species such as mouse, nematode and echiuran. The nematode enzyme is apparently involved in molting of third stage larvae (11).
- Nagler, D.K. and R. Menard (1998) FEBS Lett. 434:135.
- Santamaria, I. et al. (1998) J. Biol. Chem. 273:16816.
- Deussing, J. et al. (2000) Biochim. Biophys. Acta 1491:93.
- Pungercar, J. and G. Ivanovski (2000) Pflugers Arch. Eur. J. Physiol. 439:R116.
- Pungercar, J. et al. (2000) Pflugers Arch. Eur. J. Physiol. 439:R119.
- Sivaraman, J. et al. (2000) J. Mol. Biol. 295:935.
- Menard, R. et al. (2001) Biol. Chem. 382:839.
- Therrien, C. et al. (2001) Biochemistry 40:2702.
- Klemencic, I. et al. (2000) Eur. J. Biochem. 267:5404.
- Guncar, G. et al. (2000) Structure Fold Des. 8:305.
- Lustigman, S. et al. (1996) J. Biol. Chem. 271:30181.
Product Datasheets
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