Mouse Cathepsin C/DPPI Biotinylated Antibody

Catalog # Availability Size / Price Qty
BAF1034
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Mouse Cathepsin C/DPPI Biotinylated Antibody Summary

Species Reactivity
Mouse
Specificity
Detects mouse Cathepsin C/DPPI in Western blots. In Western blots, approximately 10% cross‑reactivity with recombinant human Cathepsin C/Cathepsin C is observed and less than 1% cross‑reactivity with recombinant mouse (rm) Cathepsin A, rmCathepsin B, rmCathepsin D, rmCathepsin H and, and rmCathepsin X/Z/P is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse Cathepsin C/DPPI
Asp25-Leu462
Accession # P97821
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Mouse Cathepsin C/DPPI (Catalog # 1034-CY)
Immunohistochemistry
5-15 µg/mL
Immersion fixed paraffin-embedded sections of human liver

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.

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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Shipping
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
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 C/DPPI

Cathepsin C is a cysteine protease of the papain family (1). Cathepsin C sequentially removes dipeptides from the free N-termini of proteins and peptides. It has broad specificity except that it does not cleave a basic amino acid (Arg or Lys) in the N-terminal position or Pro on either side of the scissle bond. It requires halide ions for activity. The pro form contains a pro peptide and a catalytic region, which can be further processed into heavy/ alpha and light/ beta chains that are linked by a disulfide bond. It is broadly distributed. Cathepsin C plays a role in the lysosomal degradation. It also functions as a key enzyme in the activation of granule serine proteases in cytotoxic T lymphocytes and natural killer cells (granzymes A and B), mast cells (tryptase and chymase), and neutrophils (Cathepsin G and elastase) by removing their N-terminal activation dipeptides (2).

References
  1. Turk, B. et al. (2004) in Handbook of Proteolytic Enzymes. Barrett, et al. eds. p. 1192, Academic Press, San Diego.
  2. Dahl, S.W. et al. (2001) Biochemistry 40:1671.
Entrez Gene IDs
1075 (Human); 13032 (Mouse); 25423 (Rat)
Alternate Names
Cathepsin C; cathepsin CEC 3.4.14.1; Cathepsin J; CPPIHMS; CTSC; dipeptidyl peptidase 1; Dipeptidyl peptidase I; Dipeptidyl transferase; dipeptidyl-peptidase I; DPP1; DPPI; DPP-I; JP; JPD; PALS; PLS

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