Datasheet

Biological Description

Specificity	Anti-Cathepsin S Rabbit Antibody [D17A22] detects endogenous levels of total Cathepsin S protein.
Background	Cathepsin S is a lysosomal cysteine protease of the papain family, synthesized as a preproenzyme and activated in acidic compartments. It consists of a 217-amino acid single polypeptide with a papain-like fold containing two domains that form the active site. Unlike many other cathepsins, it retains proteolytic activity at neutral pH, allowing it to act both intracellularly within lysosomes and extracellularly in tissue remodeling and immune responses. Its catalytic activity depends on a critical Cys25–His163 diad, while its substrate-binding cleft confers specificity for peptide cleavage. Cathepsin S plays a central role in adaptive immunity by cleaving invariant chain fragments during MHC class II maturation in antigen-presenting cells, enabling efficient peptide loading and T-cell activation. It also degrades extracellular matrix proteins such as laminin, fibronectin, collagen, and elastin, thereby regulating angiogenesis, vascular permeability, and tissue repair. It also modulates apoptosis through intrinsic mitochondrial and extrinsic death receptor pathways, regulates autophagy, and influences cell survival and homeostasis. Cathepsin S is frequently overexpressed in inflammatory and autoimmune diseases, as well as in cancers, including oral squamous cell carcinoma, where it contributes to malignant cell invasion and migration through extracellular matrix remodeling and signaling pathways.

Specificity

Anti-Cathepsin S Rabbit Antibody [D17A22] detects endogenous levels of total Cathepsin S protein.

Background

Cathepsin S is a lysosomal cysteine protease of the papain family, synthesized as a preproenzyme and activated in acidic compartments. It consists of a 217-amino acid single polypeptide with a papain-like fold containing two domains that form the active site. Unlike many other cathepsins, it retains proteolytic activity at neutral pH, allowing it to act both intracellularly within lysosomes and extracellularly in tissue remodeling and immune responses. Its catalytic activity depends on a critical Cys25–His163 diad, while its substrate-binding cleft confers specificity for peptide cleavage. Cathepsin S plays a central role in adaptive immunity by cleaving invariant chain fragments during MHC class II maturation in antigen-presenting cells, enabling efficient peptide loading and T-cell activation. It also degrades extracellular matrix proteins such as laminin, fibronectin, collagen, and elastin, thereby regulating angiogenesis, vascular permeability, and tissue repair. It also modulates apoptosis through intrinsic mitochondrial and extrinsic death receptor pathways, regulates autophagy, and influences cell survival and homeostasis. Cathepsin S is frequently overexpressed in inflammatory and autoimmune diseases, as well as in cancers, including oral squamous cell carcinoma, where it contributes to malignant cell invasion and migration through extracellular matrix remodeling and signaling pathways.

Usage Information

Application

WB, IHC

Dilution

WB	IHC
1:1000 - 1:10000	1:50 - 1:500

Reactivity

Human

Source

Rabbit

MW

37 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/22024571/
https://pubmed.ncbi.nlm.nih.gov/32668602/

Anti-Cathepsin S Rabbit Antibody [D17A22]

Biological Description

Usage Information

References

Application Data