CTSW Human

Cathepsin-W Human Recombinant
Cat. No.
BT30768
Source
Escherichia Coli.
Synonyms
Cathepsin W (Lymphopain), LYPN, lymphopain, EC 3.4.22.-.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTeks products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

CTSW Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 378 amino acids (22-376) and having a molecular mass of 42.0 kDa. CTSW is fused to a 23 amino acid His-tag at N-terminus.

Product Specs

Introduction
CTSW, a member of the peptidase C1 family, is a cysteine proteinase that plays a crucial role in regulating T-cell cytolytic activity. This protein is found within the endoplasmic reticulum membrane of natural killer and cytotoxic T-cells. Interleukin-2 stimulates the upregulation of CTSW expression.
Description
Recombinant human CTSW, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 42.0 kDa. It comprises 378 amino acids (residues 22-376) and includes a 23 amino acid His-tag fused at the N-terminus.
Physical Appearance
A clear, sterile solution that has been filtered.
Formulation
The CTSW solution is provided at a concentration of 0.5 mg/ml and is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.4 M urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
SDS-PAGE analysis indicates a purity greater than 85%.
Synonyms
Cathepsin W (Lymphopain), LYPN, lymphopain, EC 3.4.22.-.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSIRGPLRA QDLGPQPLEL KEAFKLFQIQ FNRSYLSPEE HAHRLDIFAH NLAQAQRLQE EDLGTAEFGV TPFSDLTEEE FGQLYGYRRA AGGVPSMGRE IRSEEPEESV PFSCDWRKVA GAISPIKDQK NCNCCWAMAA AGNIETLWRI SFWDFVDVSV QELLDCGRCG DGCHGGFVWD AFITVLNNSG LASEKDYPFQ GKVRAHRCHP KKYQKVAWIQ DFIMLQNNEH RIAQYLATYG PITVTINMKP LQLYRKGVIK ATPTTCDPQL VDHSVLLVGF GSVKSEEGIW AETVSSQSQP QPPHPTPYWI LKNSWGAQWG EKGYFRLHRG SNTCGITKFP LTARVQKPDM KPRVSCPP.

Product Science Overview

Introduction

Cathepsin-W, also known as lymphopain, is a cysteine protease that belongs to the peptidase C1 family of cysteine cathepsins. This enzyme is encoded by the CTSW gene in humans . Cathepsin-W is predominantly expressed in cytotoxic cells, particularly natural killer (NK) cells and cytotoxic T lymphocytes (CTLs) .

Structural Characteristics

Cathepsin-W shares structural similarities with other members of the papain-like cysteine protease family. It is characterized by its unique enzymatic activities and substrate specificity . The enzyme is glycosylated with high mannose-type glycans and is mainly localized in the endoplasmic reticulum (ER) .

Biological Functions

Cathepsin-W plays a crucial role in the immune response. It is predominantly expressed in NK cells, which are preactivated cytotoxic cells capable of mediating their effector function without depending on presented antigenic peptides (MHC class I independent) . The enzyme is also expressed in CTLs, which require activation by antigen-derived peptides bound to the MHC class I complex .

Pathological Implications

The involvement of cathepsin-W in various physiological and pathological processes is an area of active research. It has been implicated in the modulation of immune responses and may have potential roles in autoimmune and neurodegenerative diseases . Additionally, cathepsin-W is being studied for its potential as a biomarker and therapeutic target in cancer progression .

Recombinant Production

Human recombinant cathepsin-W is produced using recombinant DNA technology. This involves the insertion of the CTSW gene into an expression vector, which is then introduced into a host cell system for protein production. The recombinant enzyme is subsequently purified for research and therapeutic applications.

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