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pMD18-T Simple Vector is a high-efficiency TA cloning vector constructed from pUC18, of which the initial multiple cloning sites (MCS) were destroyed. Thus the cDNA should be amplified by PCR with primers containing a restriction site for subclone. Competent cells appropriate for pUC18 are also appropriated for the Vector, e.g. JM109, DH5α, TOP10. The pMD18-T Simple Vector is 2.6kb in size. Selection of the plasmid in E. coli is conferred by the ampicillin resistance gene. The coding sequence was inserted by TA cloning at site 425.
The coding sequence can be amplified by PCR with M13-47 and RV-M primers.
|Human CTSA ORF mammalian expression plasmid, C-GFPSpark tag||HG10482-ACG|
|Human CTSA ORF mammalian expression plasmid, C-OFPSpark / RFP tag||HG10482-ACR|
|Human CTSA ORF mammalian expression plasmid, C-Flag tag||HG10482-CF|
|Human CTSA ORF mammalian expression plasmid, C-His tag||HG10482-CH|
|Human CTSA ORF mammalian expression plasmid, C-Myc tag||HG10482-CM|
|Human CTSA ORF mammalian expression plasmid, C-HA tag||HG10482-CY|
|Human CTSA ORF mammalian expression plasmid, N-Flag tag||HG10482-NF|
|Human CTSA ORF mammalian expression plasmid, N-His tag||HG10482-NH|
|Human CTSA ORF mammalian expression plasmid, N-Myc tag||HG10482-NM|
|Human CTSA ORF mammalian expression plasmid, N-HA tag||HG10482-NY|
|Human CTSA Gene cDNA clone plasmid||HG10482-U|
|Human CTSA natural ORF mammalian expression plasmid||HG10482-UT|
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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.