Cathepsin L Protein (His tag)

Catalog No. ABIN7194682

This Recombinant Cathepsin L protein is expressed in HEK-293 Cells.

Quick Overview for Cathepsin L Protein (His tag) (ABIN7194682)

Target: Cathepsin L (CTSL1) (Cathepsin L1 (CTSL1))

Protein Type: Recombinant

Origin: Human

Source: HEK-293 Cells

Application: ELISA

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

Product Details

Purification tag / Conjugate: This Cathepsin L protein is labelled with His tag.

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

Sequence: Met 1-Val 333

Characteristics: 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.

Sterility: 0.2 μm filtered

Endotoxin Level: < 1.0 EU per μg of the protein as determined by the LAL method.

Biological Activity Comment: Not validated for activity

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Restrictions: For Research Use only

Handling

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.

Storage: 4 °C,-20 °C,-80 °C

Storage Comment: 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.

Expiry Date: 12 months

Target Details

Target: Cathepsin L (CTSL1) (Cathepsin L1 (CTSL1))

Alternative Name: Cathepsin L/CTSL

Background: 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.

Molecular Weight:

Calculated MW: 37.3 kDa

Observed MW: 37 kDa

Gene ID: 1514

NCBI Accession: NP_001903

UniProt: P07711

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