Description / CLN-2
Tripeptidyl-peptidase I (TPP1), also known as CLN2, is a lysosomal serine protease detected in all tissues examined, with highest levels shown in heart and placenta. It is an aminopeptidase that cleaves tripeptides from the free N-terminus of polypeptides and may also have endopeptidase activity. Defects in TPP1 are the cause of classical late-infantile neuronal ceroid lipofusionosis, also known as ceroid lipofusionosis neuronal 2 (CLN2), a fatal childhood neurodegenerative disease characterized by progressive visual and mental decline, motor disturbance, epilepsy, and behavioral changes.
More Information
| Size | 100 µg |
|---|---|
| Source | Mouse |
| Isotype | IgG2 |
| Clone Nr. | (#9V1) |
| Species Reactivity | Human |
| Formulation | lyophilized |
| Buffer | PBS |
| Reconstitution | Centrifuge vial prior to opening. Reconstitute the antibody with 500 µl sterile PBS and the final concentration is 200 µg/ml. |
| Stability and Storage | Lyophilized samples are stable for 2 years from date of receipt when stored at -70°C. Reconstituted antibody can be aliquoted and stored frozen at < -20°C for at least six months without detectable loss of activity. |
| Preparation | This antibody was produced from a hybridoma (mouse myeloma fused with spleen cells from a mouse) immunized with Human CLN-2 recombinant protein (also called Tripeptidyl-peptidase I) |
| Antigen | recombinant human CLN-2 |
| Application | WB |
| Synonyms | TPP1; CLN2; GIG1; LPIC; TPP-1 |
| Uniprot ID | O14773 |
| Protein RefSeq | NP_000382.3 |
| mRNA RefSeq | NM_000391.3 |