Cathepsin S Protein (CTSS) (His tag)

Catalog No. ABIN7194690

This Recombinant Cathepsin S protein is produced in HEK-293 Cells.

Quick Overview for Cathepsin S Protein (CTSS) (His tag) (ABIN7194690)

Target: Cathepsin S (CTSS)

Protein Type: Recombinant

Biological Activity: Active

Origin: Mouse

Source: HEK-293 Cells

Purity: > 90 % as determined by SDS-PAGE

Product Details

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

Purpose: Recombinant Mouse Cathepsin S/CTSS Protein (His Tag)(Active)

Sequence: Met 1-Ile 340

Characteristics: A DNA sequence encoding the full length of mouse CTSS (AAB94925.1) (Met 1-Ile 340) was expressed, with a C-terminal polyhistidine tag.

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

Biological Activity Comment: Measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVENval-WRK (Dnp)-NH2, AnaSpec, Catalog # 27114.The specific activity is >300 pmoles/min/μg.(Activation description: The enzyme achieves its activity under acidic pH)

Application Details

Restrictions: For Research Use only

Handling

Format: Lyophilized

Reconstitution: Please refer to the printed manual for detailed information.

Buffer: Lyophilized from sterile PBS, pH 7.4

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.

Target Details

Target: Cathepsin S (CTSS)

Alternative Name: Cathepsin S/CTSS

Background:

Background: Cathepsin S (CTSS), one of the lysosomal proteinases, has many important physiological functions in the nervous system, especially in process of extracellular matrix degradation and endocellular antigen presentation. CTSS is synthesized as inactive precursor of 331 amino acids consisting of a 15-aa signal peptide, a propeptide of 99 aa, and a mature polypeptide of 217 aa. It is activated in the lysosomes by a proteolytic cleavage of the propeptide. Cathepsin S is expressed in the lysosome of antigen presenting cells, primarily dendritic cells, B-cells and macrophages. Compared with other lysosomal cysteine proteases, cathepsin S has displayed some unique characteristics. Cathepsin S is most well known for its critical function in the proteolytic digestion of the invariant chain chaperone molecules, thus controlling antigen presentation to CD4+ T-cells by major histocompatibility complex (MHC) class II molecules or to NK1.1+ T-cells via CD1 Molecules. Cathepsin S also appears to participate in direct processing of exogenous antigens for presentation by MHC class II to CD4+ T-cells, or in cross-presentation by MHC class I molecules to CD8+ T-cells. In addition, although direct evidence is still lacking, in its secreted form cathepsin S is implicated in degradation of the extracellular matrix, which may contribute to the pathology of a number of diseases, including arthritis, atherosclerosis, neurological diseases and chronic obstructive pulmonary disease.

Synonym: Cathepsin S, CTSS

Molecular Weight: 37.6 kDa

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