Recombinant Mouse Cathepsin L1 (CTSL) Protein (His&Myc)

Name: Recombinant Mouse Cathepsin L1 (CTSL) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-05270P
Price: 549.6 USD
Availability: InStock

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Ctsl.

Collections: Enzymes, Featured enzyme molecules, Protease, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Cathepsin L1 (CTSL) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P06797
Target Symbol	CTSL
Synonyms	Ctsl; Ctsl1Cathepsin L1; EC 3.4.22.15; Cathepsin L; Major excreted protein; MEP; p39 cysteine proteinase) [Cleaved into: Cathepsin L1 heavy chain; Cathepsin L1 light chain]
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His&C-Myc
Target Protein Sequence	IPKSVDWREKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHAQGNQGCNGGLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEFAVANDTGFVDIPQQEKALMKAVATVGPISVAMDASHPSLQFYSSGIYYEPNCSSKNLDHGVLLVGYGYEGT
Expression Range	114-288aa
Protein Length	Partial
Mol. Weight	26.2 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Thiol protease important for the overall degradation of proteins in lysosomes (Probable). 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. In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter. 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. Secreted form generates endostatin from COL18A1. Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation. Required for maximal stimulation of steroidogenesis by TIMP1.
Subcellular Location	Lysosome. Apical cell membrane; Peripheral membrane protein; Extracellular side. Secreted, extracellular space. Secreted. Cytoplasmic vesicle, secretory vesicle, chromaffin granule.
Protein Families	Peptidase C1 family
Database References	KEGG: mmu:13039 STRING: 10090.ENSMUSP00000021933 UniGene: Mm.471755
Tissue Specificity	Expressed in thymus, kidney and liver. Expressed in thyroid epithelial cells. Expressed in cortical thymic epithelial cells. Expressed by antigen presenting cells (APCs) such as dendritic cells and macrophages.

Gene Functions References

findings suggest that CTSL contributes to the proliferation and metastasis of breast cancer and might be a potent molecular target for breast cancer treatment PMID: 26639231
causally involved in the pathogenesis of experimental diabetic nephropathy PMID: 27575559
findings suggest that single chain-cathepsin L is biologically active in promoting Th17 generation and is counter-regulated by serpinB1 and secondarily by asparagine endopeptidase. PMID: 26343333
CTSL plays an important role in the MHC class II-mediated peptide presentation in thymic epithelial cells, acting both in the invariant chain degradation and in the generation of MHC class II-bound peptide ligands presented by cortical thymic epithelial cells. Consequently, CTSL plays an important role in the positive selection of CD4+ T cell in thymus. PMID: 11119260
genetic blockade of cathepsin L activity is inferred to retard Myc-driven tumor growth, encouraging the potential utility of pharmacological inhibitors of cysteine cathepsins in treating late stage tumors. PMID: 25927437
The phenotypes of cathepsin L deficiency can be fully assigned to lack of canonically targeted cathepsin L, while the biogenesis and functionality of nucleo-cytosolic cathepsin L remain elusive. PMID: 25222295
in vivo functional evidence for overexpressed CTSL as a promoter of lung metastasis, whereas high CTSL levels are maintained during tumor progression due to stress-resistant mRNA translation. PMID: 25957406
cathepsin L has a protective role in mouse skin carcinogenesis PMID: 21538579
Cathepsin L is involved in nociception in mice, whereas peripheral autophagy and cathepsin L contribute, at least in part, to the antinociceptive effect of dimethoxybenzylidene in mice. PMID: 23912553
a degradative Ctsl-MMP-2 axis, resulting in increased MMP-2 levels upon cathepsin deficiency with subsequent degradation of secreted proteins such as collagen alpha-1 (I). PMID: 23811845
Cathepsin L protects mice from mycoplasmal infection and is essential for airway lymphangiogenesis. PMID: 23600672
B-cell lymphopoiesis is regulated by cathepsin L. PMID: 23585893
Lysosomal CTSL attenuates cardiac hypertrophy and preserves cardiac function through facilitation of autophagy and proteasomal protein processing. PMID: 23608608
Two new thyroiditogenic thyroglobulin (Tg)epitopes are located near cathepsin L cleavage sites, clustered close to known immunopathogenic Tg epitopes. PMID: 23315080
Bushen tiaojing recipe and xiaoyao pill promoted ovulation by enhancing the expression of CatL. PMID: 21434350
Cathepsins L and Z are critical in degrading polyglutamine-containing proteins within lysosomes. PMID: 22451661
Cathepsin L contributes to abdominal aortic aneurysms formation by promoting lesion inflammatory cell accumulation, angiogenesis, and protease expression. PMID: 21868704
Cathepsin L deficiency affects, albeit in a limited manner, the abundances of extracellular matrix (ECM) components, signaling proteins, and further proteases as well as endogenous protease inhibitors. PMID: 21972973
Defects in DNA repair associated with 53BP1 deficiency upon loss of A-type lamins are due to upregulation of CTSL. PMID: 21750527
Cathepsin L deficiency significantly reduced lung granuloma number in a mouse model of sarcoidosis. PMID: 21251246
CTSL regulates cardiac repair and remodelling post-myocardial infarction through a mechanism with multiple pathways. PMID: 21147810
Downregulation of cathepsin L prevents autoimmune diabetes via suppression of CD8(+) T cell activity. PMID: 20877570
Data from studies using embryonic cells from Ctsl knockout mice confirm Ctsl as a major protease involved in turnover of phagosomes/lysosomes. PMID: 20536383
Granule-bound cathepsins are essential for processing perforin to its active form, and that CatL is an important, but not exclusive, participant in this process. PMID: 20497254
cathepsin L expressed in endothelial progenitor cells plays a critical role in intraocular angiogenesis PMID: 20304958
conclude that a tightly regulated balance between cathepsin L and cystatin M/E is essential for tissue integrity in epidermis, hair follicles, and corneal epithelium PMID: 20495178
NOD knock-out mice exhibit complete resistance to diabetes PMID: 19664906
These results demonstrate a prominent role for cathepsin L, jointly with PC1/3 and PC2, for production of dynorphins in brain. PMID: 19837164
Data suggest that Ctsl is critical for the termination of growth factor signaling in the endosomal/lysosomal compartment of keratinocytes and, therefore, functions as an anti-tumor protease. PMID: 20023699
In mouse models of pancreatitis, absence of cathepsin L induces apoptosis and reduces disease severity. PMID: 19900452
Results suggest that cathepsin L functions as a major protease responsible for CCK8 production in mouse brain cortex, and participates with PC1/3 for CCK8 production in pituitary cells. PMID: 19589362
For a subset of antigens, epitope generation is critically regulated by cathepsin L, which participates in antigen processing and generates qualitative and quantitative differences in the peptide repertoires displayed by MHC class II molecules. PMID: 11884425
An alternate targeting pathway for procathepsin L in mouse fibroblasts PMID: 11929604
Dilated cardiomyopathy in mice deficient for the lysosomal cysteine peptidase cathepsin L. PMID: 11972068
cathepsin L is the primary mediator of reovirus disassembly PMID: 11986312
Cathepsin L regulates CD4+ T cell selection independently of its effect on invariant chain: a role in the generation of positively selecting peptide ligands PMID: 12021314
mice lacking cathepsin L have neuronal loss and brain atrophy; demonstrates pivotal role in maintenance of the central nervous system PMID: 12048238
shows evolution in placental expression by gene duplication PMID: 12054558
cathepsin L plays a critical role in hair follicle morphogenesis and cycling, as well as epidermal differentiation PMID: 12163394
regulation of the phagosomal CatL, CatB, CatS ans CatZ contents during dendritic cell activation PMID: 12186844
Studies of thymocytes from knockout mice demonstrate a specific role for catL in regulating presentation of natural CD1d ligands mediating V(alpha)14(+)NK1.1(+) T cell selection. PMID: 12368909
major histocompatibility complex class II-associated invariant chain controls the activity of extracellular cathepsin L PMID: 12417635
Data show that impaired cathepsin-L function may lead to the establishment of gingival overgrowth as seen in patients treated with calcium antagonists. PMID: 12466121
Prevents atrophy of seminiferous tubules and promotes the formation of preleptotene spermatocytes and the differentiation of these meiotic cells into pachytene spermatocytes. PMID: 12533435
cathepsin L plays a regulatory role early in the process of mammary gland involution PMID: 12815617
Cathepsin L has an previously uncharacterized biological role in the production of [Met]enkephalin, an endogenous peptide neurotransmitter PMID: 12869695
muscle cathepsin L gene expression is increased in diabetes-prone mice and related to glucose tolerance. PMID: 12941783
A cathepsin L isoform devoid of a signal peptide loalizes to the nucleus in S phase and processes the CDP/Cux transcription factor. PMID: 15099520
cathepsin L and alpha(3) integrin have roles in podocyte migration PMID: 15197181
Data suggest that cathepsin L has a critical role in the integration of circulating endothelial progenitor cells (EPC) into ischemic tissue and is required for EPC-mediated neovascularization. PMID: 15665831

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Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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