Detects mouse Cathepsin X/Z/P in direct ELISAs and Western blots. In direct ELISAs, approximately 40% cross-reactivity with recombinant human Cathepsin X/Z/P is observed and less than 2% cross-reactivity with recombinant mouse Cathepsin B, C, D, H, and L is observed.
Measured by its ability to neutralize Recombinant Mouse Cathepsin X/Z/P (0.1 µg/mL, Catalog # 1033-CY) cleavage of the fluorogenic peptide substrate Mca-RPPGFSAFK(Dnp)-OH (10 µM, Catalog # ES005). The Neutralization Dose (ND50) is typically 2.0 µg/mL.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Cathepsin X/Z/P in Mouse Splenocytes.
Cathepsin X/Z/P was detected in immersion fixed mouse splenocytes using Goat Anti-Mouse Cathepsin X/Z/P Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1033) at 15 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Goat IgG Secondary Antibody (red; Catalog # NL001) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm. View our protocol for Fluorescent ICC Staining of Non-adherent Cells.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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 relatively new 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).
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R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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