Recombinant Rat Procathepsin L (Ctsl), partial

Code CSB-YP006193RA
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Source Yeast
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Code CSB-EP006193RA
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Source E.coli
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Code CSB-EP006193RA-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP006193RA
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Source Baculovirus
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Code CSB-MP006193RA
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Ctsl
Uniprot No.
Alternative Names
Ctsl; Ctsl1Cathepsin L1; EC 3.4.22.15; Cathepsin L; Cyclic protein 2; CP-2; Major excreted protein; MEP) [Cleaved into: Procathepsin L; Cathepsin L1 heavy chain; Cathepsin L1 light chain]
Species
Rattus norvegicus (Rat)
Expression Region
114-288aa
Target Protein Sequence
IPKTVDWREKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHDQGNQGCNGGLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEYAVANDTGFVDIPQQEKALMKAVATVGPISVAMDASHPSLQFYSSGIYYEPNCSSKDLDHGVLVVGYGYEGT
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Thiol protease important for the overall degradation of proteins in lysosomes. 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. 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.
Gene References into Functions
  1. the activation of cathepsin L contributes to the irreversible depolarization produced by oxygen and glucose deprivation PMID: 27818353
  2. Cathepsins in Rotator Cuff Tendinopathy: Identification in Human Chronic Tears and Temporal Induction in a Rat Model. PMID: 25558848
  3. Inhibition of the activation of cathepsin L contributes to neuroprotection against cerebral ischemia. PMID: 24616078
  4. Changes in olfaction were less consistent and widespread in the hippocampus, but were again sex specific for three genes: cathepsin-L (CtsL), matrix metalloproteinase-14 (MMP-14) and MMP-16. PMID: 23103411
  5. With aging, the level of cathepsin L delined at 18 month but rose at 24 month in brain. PMID: 21374014
  6. double transgenic rats (human renin and angiotensinogen genes) were used to investigate sex differences influencing renal function and gene expression. Cathepsin L was differentially expressed between the sexes and associated with degree of renal injury. PMID: 21357272
  7. confirmed 6-hydroxydopamine induced nuclear translocation of cathepsin L in rat substantia nigral neurons as well PMID: 21134415
  8. study found, in differentiated PC12 cells, lysosomal membrane permeabilization is an early event in palmitic acid-induced lipotoxicity preceeding mitochondrial membrane permeabilization & apoptosis; cathepsin L is an important contributor in this process PMID: 20043885
  9. shows evolution in placental expression PMID: 12054558
  10. the GC-box is a critical regulatory element for the cathepsin L promoter in mature Sertoli cells PMID: 12606333
  11. data document that three Sp1/specificity protein 3 binding regions and a functional cyclic amp regulatory element constitute an important transcriptional regulatory complex for expression of the cathepsin L gene in rat granulosa cells PMID: 14563703
  12. The induction of puromycin aminonucleoside nephrosis involves podocyte migration conducted by a coordinated interplay between the cysteine protease cathepsin L and alpha(3) integrin PMID: 15197181
  13. endothelial cell-associated cathepsins B and L are not involved in the invasive growth of capillaries from existing blood vessels and the presence of collagen is necessary for MMP2 expression in endothelial cells PMID: 15255544
  14. The co-localization of PAP/TRAP and the cysteine protease cathepsin L could suggest a role for cathepsin L in the in vivo proteolytic processing of PAP/TRAP. PMID: 15761664
  15. Results show Cathepsin L plays a critical role in the lysosomal degradation of L-lactate dehydrogenase. PMID: 16960372
  16. Our data strongly suggests that the decrease in heat shock protein levels and the significant reduction of serum albumin leakage into the brain following acute treatment with CP-1 is indicative of less secondary ischemic damage. PMID: 18060871
  17. Study indicates that CTSL improves cardiac function and inhibits cardiac hypertrophy, inflammation, and fibrosis through blocking Akt/GSK3beta signaling. PMID: 19096818
  18. Upstream repressors and activators as well as cis-acting elements near the transcription start site control stage-specific Ctsl transcription by Sertoli cells. PMID: 19458314

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Subcellular Location
Lysosome. Apical cell membrane; Peripheral membrane protein; Extracellular side. Cytoplasmic vesicle, secretory vesicle, chromaffin granule. Secreted, extracellular space. Secreted.
Protein Families
Peptidase C1 family
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.
Database Links
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301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
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7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
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