Mouse Cathepsin C/DPPI Biotinylated Antibody

Catalog #: BAF1034 Datasheet / COA / SDS

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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.

Reconstitution Calculator

Preparation and Storage

Reconstitution

Reconstitute at 0.2 mg/mL in sterile PBS.

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

Turk, B. et al. (2004) in Handbook of Proteolytic Enzymes. Barrett, et al. eds. p. 1192, Academic Press, San Diego.
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