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SRP0291

Sigma-Aldrich

Cathepsin L Active human

recombinant, expressed in FreeStyle 293-F cells, ≥90% (SDS-PAGE)

Sinonimo/i:

CATL, Major excreted protein (MEP)

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About This Item

Codice UNSPSC:
12352204
NACRES:
NA.54

Origine biologica

human

Ricombinante

expressed in FreeStyle 293-F cells

Saggio

≥90% (SDS-PAGE)

Forma fisica

aqueous solution

Attività specifica

≥3900 pmol/min-μg

PM

36 kDa

tecniche

inhibition assay: suitable

Compatibilità

suitable for molecular biology

N° accesso NCBI

applicazioni

life science and biopharma

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Informazioni sul gene

human ... CTSL(1514)

Descrizione generale

Research area: Cell Signaling

Cathepsin L is a papain-like cysteine protease and belongs to the Clan A, Family C1. It is composed of L domain of α-helix and an R domain of β-sheet in the spatial structure.

Human cathepsin L (GenBank Accession No. NM_001912), amino acids 18-333, with C-terminal HIS tag, MW = 36 kDa, expressed in FreeStyle 293-F cells.

Applicazioni

Active human cathepsin L is useful for the activation of DPP1 (Cathepsin C). Active human cathepsin L has been used:
  • to determine that N-acyl and N-sulfonyloxazolidine-2,4-diones are pseudo-irreversible inhibitors of serine proteases
  • to investigate the role of cathepsin B and L activity in the serum during the human aging process.
  • in inhibitory activity assay
  • to study the role of CTSL in COVID-19 infection

Azioni biochim/fisiol

Cathepsin L is a cysteine protease, involved primarily in protein breakdown in the lysosome. Cathepsin L degrades nuclear transcription factors and may affect cell cycle regulation. Cathepsin L is also involved in the immune system, specifically in degrading the invariant chain during major histocompatibility complex (MHC) class II processing, a crucial step in antigen presentation. Its expression in the thymus has been demonstrated to be vital for the development of natural killer cells. Additionally, Cathepsin L contributes to recycling processes during axon outgrowth and synapse formation in the developing postnatal central nervous system. Proteases are associated with the development and progression of cancer. Therefore, cathepsin L may be a potential therapeutic target in cancer treatment.

Definizione di unità

One unit is defined as the amount of enzyme that will cleave 1 pmol of substrate per min at 37°C

Stato fisico

Formulated in 50 mM MES, 400 mM NaCl, pH 5.0, and 10% glycerol.

Nota sulla preparazione

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

Note legali

FreeStyle is a trademark of Invitrogen Corp.

Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Ricardo A Orbegozo-Medina et al.
PloS one, 14(2), e0211035-e0211035 (2019-02-02)
Recombinant proteins expressed in E. coli are frequently purified by immobilized metal affinity chromatography (IMAC). By means of this technique, tagged proteins containing a polyhistidine sequence can be obtained up to 95% pure in a single step, but some host
Jana Ilgová et al.
Molecular and biochemical parasitology, 235, 111248-111248 (2019-12-25)
The gills of the common carp, whose mucosal surface belongs to the key defence mechanisms of piscine immunity, can be infested with both the larval and adult stage of Eudiplozoon nipponicum (Monogenea). Although on their own, monogeneans do not considerably
Jacqueline M Lankelma et al.
Life sciences, 86(7-8), 225-233 (2009-12-05)
Cathepsin L, a cysteine protease, is considered to be a potential therapeutic target in cancer treatment. Proteases are involved in the development and progression of cancer. Inhibition of activity of specific proteases may slow down cancer progression. In this review
Prohormone Thiol Protease
Vivian Y.H. Hook
Handbook of Proteolytic Enzymes (2013)
Heather S Davies et al.
Analytical chemistry, 88(23), 11609-11615 (2016-10-30)
The major structural components of protective mucus hydrogels on mucosal surfaces are the secreted polymeric gel-forming mucins. The very high molecular weight and extensive O-glycosylation of gel-forming mucins, which are key to their viscoelastic properties, create problems when studying mucins

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