Cathepsin A / CTSA Recombinant Protein | CTSA recombinant protein

Recombinant Human Cathepsin A / CTSA Protein (His tag)

Cat. Num. AAA2546229

• Gene Names: CTSA; GSL; GLB2; NGBE; PPCA; PPGB
• Purity: > 90 % as determined by SDS-PAGE
• Synonyms: Cathepsin A / CTSA; Recombinant Human Cathepsin A / CTSA Protein (His tag); CTSA; RP3-337O18.1; GLB2; GSL; NGBE; PPCA; PPGB; CTSA recombinant protein

• Host: Human Cells
• Purity/Purification: > 90 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile 25mM Tris, 0.15mM NaCl, pH 7.5
• Sequence Length: 480

• Application Notes: The secreted recombinant human CTSA existing as a single-chain form consists of 463 amino acids and has a predicted molecular mass of 53 kDa as estimated by SDS-PAGE under reducing conditions.
• Predicted N Terminal: Ala 29
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

Related Product Information for CTSA recombinant protein

Background: Lysosomal carboxypeptidase, cathepsin A (protective protein, CathA), is a component of the lysosomal multienzyme complex along with beta-galactosidase (GAL) and sialidase Neu1, where it activates Neu1 and protects GAL and Neu1 against the rapid proteolytic degradation. Cathepsin A is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities. It was recently identified in human platelets as deamidase. In vitro, it hydrolyzes a variety of bioactive peptide hormones including tachykinins, suggesting that extralysosomal cathepsin A plays a role in regulation of bioactive peptide functions. It is a member of the alpha/beta hydrolase fold family and has been suggested to share a common ancestral relationship with other alpha/beta hydrolase fold enzymes, such as cholinesterases. Cathepsin A defects are linked to multiple forms of Galactosialidosis with a combined secondary deficiency of beta-galactosidase and neuraminidase. Cathepsin A is a key molecule in the onset of galactosialidosis and also highlight the therapeutic acts in vivo as an endothelin-1-inactivating enzyme and strongly confirm a crucial role of this enzyme in effective elastic fiber formation.

Description: A DNA sequence encoding the human cathepsin A isoform b (Met 1-Tyr 480) (NP_001121167.1) was expressed with a N-terminal signal peptide and a C-terminal polyhistidine tag.

NCBI and Uniprot Product Information

• NCBI GI #: 189163485
• NCBI GeneID: 5476
• NCBI Accession #: NP_001121167.1
• NCBI GenBank Nucleotide #: NM_001127695.2
• UniProt Accession #: P10619; Q561W6; Q5JZH1; Q96KJ2; Q9BR08; Q9BW68; B2R798
• Molecular Weight: 52,489 Da
• NCBI Official Full Name: lysosomal protective protein isoform b preproprotein
• NCBI Official Synonym Full Names: cathepsin A
• NCBI Official Symbol: CTSA
• NCBI Official Synonym Symbols: GSL; GLB2; NGBE; PPCA; PPGB
• NCBI Protein Information: lysosomal protective protein
• UniProt Protein Name: Lysosomal protective protein
• Protein Family: Lysosomal protective protein
• UniProt Gene Name: CTSA
• UniProt Synonym Gene Names: PPGB; PPCA

NCBI Description

This gene encodes a member of the peptidase S10 family of serine carboxypeptidases. Alternative splicing results in multiple transcript variants, at least one of which encodes a preproprotein that is proteolytically processed to generate two chains that comprise the heterodimeric active enzyme. This enzyme possesses deamidase, esterase and carboxypeptidase activities and acts as a scaffold in the lysosomal multienzyme complex. Mutations in this gene are associated with galactosialidosis. [provided by RefSeq, Nov 2015]

Uniprot Description

CTSA: Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. Defects in CTSA are the cause of galactosialidosis (GSL). A lysosomal storage disease associated with a combined deficiency of beta-galactosidase and neuraminidase, secondary to a defect in cathepsin A. All patients have clinical manifestations typical of a lysosomal disorder, such as coarse facies, cherry red spots, vertebral changes, foam cells in the bone marrow, and vacuolated lymphocytes. Three phenotypic subtypes are recognized. The early infantile form is associated with fetal hydrops, edema, ascites, visceromegaly, skeletal dysplasia, and early death. The late infantile type is characterized by hepatosplenomegaly, growth retardation, cardiac involvement, and a normal or mildly affected mental state. The juvenile/adult form is characterized by myoclonus, ataxia, angiokeratoma, mental retardation, neurologic deterioration, absence of visceromegaly, and long survival. Belongs to the peptidase S10 family.

Protein type: EC 3.4.16.5; Endoplasmic reticulum; Mitochondrial; Protease

Chromosomal Location of Human Ortholog: 20q13.12

Cellular Component: endoplasmic reticulum; intracellular membrane-bound organelle; lysosomal lumen; membrane; nucleoplasm

Molecular Function: carboxypeptidase activity; enzyme activator activity; exo-alpha-sialidase activity; serine carboxypeptidase activity

Biological Process: glycosphingolipid metabolic process; intracellular protein transport; proteolysis; proteolysis involved in cellular protein catabolic process; regulation of protein stability

Disease: Galactosialidosis