Recombinant Human Cathepsin L/MEP protein (His tag N-Terminus)
Recombinant Human Cathepsin L/MEP protein (His tag N-Terminus)
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Recombinant Human Cathepsin L/MEP protein (His tag N-Terminus) is a Human Full Length protein, in the 18 to 333 aa range, expressed in Escherichia coli, with >85%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
別名を表示する
CTSL1, CTSL, Procathepsin L, Cathepsin L1, Major excreted protein, MEP
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Cathepsin L/MEP protein (His tag) (AB222993)
3μg of ab222993 was analysed by 15% SDS-PAGE.
Reactivity data
配列情報
出荷温度及び保存条件
出荷温度
短期保存期間
短期保存温度
長期保存温度
分注に関する情報
保管に関する情報
補足情報
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Cathepsin L links to cellular homeostasis and extracellular matrix remodeling. It often acts in protein turnover and antigen processing within endolysosomal compartments making it essential for major histocompatibility complex class II presentation. Cathepsin L forms complexes in certain conditions playing roles in interacting and modifying other proteins. It controls processes essential for cell survival differentiation and apoptosis.
Pathways
Cathepsin L plays significant roles in pathways like apoptosis and autophagy. It coordinates with other proteases and proteins such as cathepsin B and cathepsin S to regulate cell death and survival. In apoptosis cathepsin L mediates the breakdown of cellular components working alongside caspases. Its interaction with autophagy involves degradation of long-lived proteins highlighting its role in recycling amino acids during stress conditions.
製品の性状
製品の状態
Liquid
補足情報
Purified using conventional chromatography techniques.
一般的な情報
機能
Thiol protease important for the overall degradation of proteins in lysosomes (Probable). 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 (By similarity). 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 (PubMed : 10716919). 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 (By similarity).. (Microbial infection) In cells lacking TMPRSS2 expression, facilitates human coronaviruses SARS-CoV and SARS-CoV-2 infections via a slow acid-activated route with the proteolysis of coronavirus spike (S) glycoproteins in lysosome for entry into host cell (PubMed : 16339146, PubMed : 18562523, PubMed : 32142651, PubMed : 32221306, PubMed : 37990007). Proteolysis within lysosomes is sufficient to activate membrane fusion by coronaviruses SARS-CoV and EMC (HCoV-EMC) S as well as Zaire ebolavirus glycoproteins (PubMed : 16081529, PubMed : 18562523, PubMed : 26953343).. Isoform 2. Functions in the regulation of cell cycle progression through proteolytic processing of the CUX1 transcription factor (PubMed : 15099520). Translation initiation at downstream start sites allows the synthesis of isoforms that are devoid of a signal peptide and localize to the nucleus where they cleave the CUX1 transcription factor and modify its DNA binding properties (PubMed : 15099520).
配列の類似性
Belongs to the peptidase C1 family.
翻訳後修飾
During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (By similarity). Autocleavage; produces the single-chain CTSL after cleavage of the propeptide. The cleavage can be intermolecular (PubMed:9468501).
細胞内局在性
Lysosome
ターゲットの情報
組合せ製品
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