Anti-Cathepsin L Antibody (Monoclonal, 33/2)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-F |
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Primary Accession | P07154 |
Host | Mouse |
Isotype | Mouse IgG1 |
Reactivity | Human, Mouse, Rat |
Clonality | Monoclonal |
Format | Lyophilized |
Description | Mouse IgG monoclonal antibody for Cathepsin L, cathepsin L1 (CTSL1) detection. Tested with WB, IHC-F in Human;mouse;rat. No cross reactivity with other proteins. |
Reconstitution | Add 1ml of PBS buffer will yield a concentration of 100ug/ml. |
Gene ID | 25697 |
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Other Names | Cathepsin L1, 3.4.22.15, Cathepsin L, Cyclic protein 2, CP-2, Major excreted protein, MEP, Procathepsin L, Cathepsin L1 heavy chain, Cathepsin L1 light chain, Ctsl, Ctsl1 |
Calculated MW | 37660 MW KDa |
Application Details | Immunohistochemistry(Frozen Section), 4 µg/ml, Human, mouse, rat, - Western blot, 2 µg/ml, Human, mouse, rat |
Subcellular Localization | Lysosome . |
Tissue Specificity | Both mature cathepsin L1 and procathepsin L are found in the upper epidermis. The lower epidermis predominantly contains procathepsin L. In seminiferous tubules expression is greater at stages VI-VII than at stages IX-XII. . |
Protein Name | Cathepsin L1 |
Contents | Mouse ascites fluid, 1.2% sodium acetate, 2mg BSA, with 0.01mg NaN3 as preservative. |
Clone Names | 33/2 |
Immunogen | Procathepsin L isolated from the human lung cancer cell line EPLC 32M1. |
Purification | Ascites |
Cross Reactivity | No cross reactivity with other proteins |
Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
Sequence Similarities | Belongs to the peptidase C1 family. |
Name | Ctsl {ECO:0000312|RGD:2448} |
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Synonyms | Ctsl1 |
Function | Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (By similarity). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (PubMed:7777858). |
Cellular Location | Lysosome. Apical cell membrane {ECO:0000250|UniProtKB:P06797}; Peripheral membrane protein {ECO:0000250|UniProtKB:P06797}; Extracellular side {ECO:0000250|UniProtKB:P06797}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P25975}. Secreted, extracellular space {ECO:0000250|UniProtKB:P06797}. Secreted. Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages. {ECO:0000250|UniProtKB:P06797} |
Tissue Location | Both mature cathepsin L1 and procathepsin L are found in the upper epidermis. The lower epidermis predominantly contains procathepsin L. In seminiferous tubules expression is greater at stages VI-VII than at stages IX-XII. |
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Background
Cathepsin L is a lysosomal cysteine proteinase with a major role in intracellular protein catabolism. It also shows the most potent collagenolytic and elastinolytic activity in vitro of any of the cathepsins. Cathepsin L has been implicated in pathologic processes including myofibril necrosis in myopathies and in myocardial ischemia, and in the renal tubular response to proteinuria. Human liver cathepsin L consists of a heavy chain of about 25 kD and a light chain of about 5 kD. The gene is mapped to 9q21-q22. Cathepsin L is required for endothelial progenitor cell-induced neovascularization.
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