Cathepsin A Protein, Human, Recombinant (His Tag)
Product Specifications
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.
Synonyms
GLB2 Protein, Human; GSL Protein, Human; NGBE Protein, Human; PPCA Protein, Human; PPGB Protein, Human
Gene Name
Cathepsin A
Expression System
HEK293 Cells
Tag
C-His
Field of Research
Serine Proteases and Regulators
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method.
Purity
> 90 % as determined by SDS-PAGE.
Activity
At Leading Biology, the biological activity of a recombinant protein is routinely measured using a bioassay, e.g. chemotaxis or cell proliferation assay, enzyme assay, or a functional ELISA. When a recombinant protein is an enzyme, specific activity is derived from an enzymatic assay. Each enzyme is tested for potency by cleavage of a substrate. We are in the process of updating the biological activity data. If you have any questions regarding this update, please feel free to contact our technical support team.
Form
Lyophilized
Buffer
Lyophilized from sterile 25mM Tris, 0.15mM NaCl, pH 7.5 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
Function
Enzyme Proteins
Molecular Weight
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.
Storage Conditions
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise. Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.
Product Datasheet
http://www.leading-biology.com/en/fastadmin/public/data/datasheet/S_Protein_datasheet/PH52485M2.pdf
Symbol
CTSA
Species
Human
Protein ID
NP_001121167.1
Overview
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.
AA Sequence
Met1-Tyr480
Protein ID Link
https://www.ncbi.nlm.nih.gov/protein/NP_001121167.1
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