Cathepsin L Protein (His tag)

N° du produit ABIN7194682

Cette protéine Recombinant Cathepsin L est exprimée dans HEK-293 Cells.

Aperçu rapide pour Cathepsin L Protein (His tag) (ABIN7194682)

Antigène: Cathepsin L (CTSL1) (Cathepsin L1 (CTSL1))

Type de proteíne: Recombinant

Origine: Humain

Source: HEK-293 Cells

Application: ELISA

Pureté: > 90 % as determined by reducing SDS-PAGE.

Détail du produit

Purification/Conjugué: Cette Cathepsin L protéine est marqué à la His tag.

Fonction: Recombinant Human Cathepsin L/CTSL Protein (His Tag)

Séquence: Met 1-Val 333

Attributs du produit: A DNA sequence encoding the pro form of human Cathepsin-L1 (NP_001903.1) (Met 1-Val 333) was expressed, fused with a polyhistidine tag at the C-terminus.

Stérilité: 0.2 μm filtered

niveau d'endotoxine: < 1.0 EU per μg of the protein as determined by the LAL method.

Biological Activity Comment: Not validated for activity

Information d'application

Indications d'application: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Stockage

Format: Lyophilized

Buffer: Lyophilized from sterile 50 mM NaAc, 0.1M NaCl, pH 5.0
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween 80 are added as protectants before lyophilization.

Stock: 4 °C,-20 °C,-80 °C

Stockage commentaire: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Date de péremption: 12 months

Détail du antigène

Antigène: Cathepsin L (CTSL1) (Cathepsin L1 (CTSL1))

Autre désignation: Cathepsin L/CTSL

Sujet: CTSL,CTSL1,Cathepsin L1,MEP,Major Excreted Protein,Cathepsin L is a lysosomal cysteine protease that plays a major role in intracellular protein catabolism, and is potent in degrading collagen, laminin, elastin, as well as alpha-1 protease inhibitor and other structural proteins of basement membranes. Like many proteases, Cathepsin L is synthesized as an inactive preproenzyme, and cleavage of the 96-residue proregion is necessary to generate the fully active 221-residue mature enzyme. Studies have demonstrated that cleavage of the proregion occur autocatalytically under acidic conditions. The enzyme takes part in nutrient acquisition by catabolizing host proteins to absorbable peptides, facilitates the migration of the parasite through the host intestine and liver by cleaving interstitial matrix proteins such as fibronectin, laminin and native collagen and is implicated in the inactivation of host immune defenses by cleaving immunoglobulins. Recently, Cathepsin L has been shown to suppress Th1 immune response in infected laboratory animals making them susceptible to concurrent bacterial infections. Cathepsin L is synthesized in large amounts and secreted by many malignantly transformed cells, and induced by growth factors and tumor promoters. In addition to its role in protein degradation, evidence has accumulated for the participation of Cathepsin L in various physiological and pathological processes, such as tumor invasion and metastasis, bone resorption, spermatogenesis, and arthritis. Accordingly, Cathepsin L may prove useful as a diagnostic or prognostic marker of human tumor malignancy.

Poids moléculaire:

Calculated MW: 37.3 kDa

Observed MW: 37 kDa

ID gène: 1514

NCBI Accession: NP_001903

UniProt: P07711

Pathways: Activation of Innate immune Response, Toll-Like Receptors Cascades