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CTSA encodes a glycoprotein which associates with lysosomal enzymes beta-galactosidase and neuraminidase to form a complex of high molecular weight multimers. Additionally we are shipping Cathepsin A Proteins (24) and Cathepsin A Kits (15) and many more products for this protein.
Showing 10 out of 84 products:
Human Polyclonal CTSA Primary Antibody for ELISA, WB - ABIN1536139
Galjart, Gillemans, Harris, van der Horst, Verheijen, Galjaard, dAzzo: Expression of cDNA encoding the human "protective protein" associated with lysosomal beta-galactosidase and neuraminidase: homology to yeast proteases. in Cell 1988
Show all 2 references for ABIN1536139
Human Polyclonal CTSA Primary Antibody for EIA, IHC (p) - ABIN951063
Reich, Spindler, Burret, Kalbacher, Boehm, Burster: Cathepsin A is expressed in primary human antigen-presenting cells. in Immunology letters 2010
Show all 2 references for ABIN951063
Mouse (Murine) Polyclonal CTSA Primary Antibody for ELISA - ABIN2000809
Hiraiwa: Cathepsin A/protective protein: an unusual lysosomal multifunctional protein. in Cellular and molecular life sciences : CMLS 2001
Human Polyclonal CTSA Primary Antibody for IHC (p), WB - ABIN654433
Hossain, Higaki, Shinpo, Nanba, Suzuki, Ozono, Sakai: Chemical chaperone treatment for galactosialidosis: Effect of NOEV on ?-galactosidase activities in fibroblasts. in Brain & development 2015
It is shown by dot-immunoblotting that At3g52840 is the gene expressing Gal-2 (show LGALS2 Antibodies) which is associated with the cell wall in Arabidopsis.
Galactosialidosis is a rare lysosomal storage disease caused by a combined deficiency of GM1 beta-galactosidase (beta-gal (show GLB1 Antibodies)) and neuraminidase (show NEU Antibodies) secondary to a defect of a lysosomal enzyme protective protein/cathepsin A (PPCA) and mutation in CTSA gene.
Case Report: galactosialidosis with novel mutations of CTSA gene diagnosed using placental pathology.
We identified compound heterozygous mutations in the CTSA gene, responsible for causing galactosialidosis
correct nomenclature of mutations for this gene is discussed; clinical and mutational analyses of 4 cases with rare infantile form of galactosialidosis; identified 3 novel nucleotide changes, 2 resulting in missense mutations and the third, resulting in the p.Gln406* stop codon; complexity of the clinical phenotypes in GS reflects dual functions of PPCA/CTSA
Catalytic function, tissue distribution and substrates of cathepsin A are discussed as well as inhibition of cathepsin A as an emerging strategy for the treatment of heart failure.
The Cathepsin C (show CTSC Antibodies) releases the glycosidases from complexes formed with cathepsin A, and reinstates their activity.
Our data suggest that CatA (show CAT Antibodies) is involved in the C-terminal fine-tuning of antigenic T cell epitopes in human APC (show APC Antibodies).
Increased activity of beta-galactosidase (show GLB1 Antibodies) in the peritoneal fluid is associated with gynecologic cancers and pelvic inflammatory disease
effects of GLB1 (show GLB1 Antibodies), PPCA and NEU1 (show NEU1 Antibodies) gene mutations on elastogenesis in skin fibroblasts
Results describe the hydrodynamic properties of PPCA, NEU1 (show NEU1 Antibodies), and a complex of the two proteins and identified multiple binding sites on both proteins.
our results define the biological role of mammalian serine carboxypeptidase Scpep1 (show SCPEP1 Antibodies) and suggest that Scpep1 (show SCPEP1 Antibodies) and CathA together participate in the control of ET-1 (show EDN1 Antibodies) regulation of vascular tone and hemodynamics
Loss of the cathepsin A results in the lysosomal storage disease galactosialidosis. However, mice with a catalytically inactive cathepsin A enzyme show no signs of this disease.
characterization of human PPCA, including N-terminal sequencing of the two cleavage products
the compromised halo cells, due to PPCA deficiency within their lysosomes, cannot function properly and as a result there is a recruitment of macrophages in the intertubular space
PPCA deficiency causes structural changes to the blood-epididymal barrier as evidenced by lanthanum nitrate and Cldns expression that affects the luminal environment of the epididymis, resulting in altered sperm motility.
CathA acts in vivo as an endothelin-1 (show EDN1 Antibodies)-inactivating enzyme and strongly confirm a crucial role of this enzyme in effective elastic fiber formation.
Results indicate a novel role for PPCA/cathepsin A in osteoclastogenesis via down-regulation of NF-kappaB p50 (show NFKB1 Antibodies)/p65 (show NFkBP65 Antibodies) activity and suggest a new function for PPCA as an NF-kappaB (show NFKB1 Antibodies)-degrading enzyme in addition to its known multifunctional properties.
Results describe the hydrodynamic properties of PPCA, NEU1 (show NEURL Antibodies), and a complex of the two proteins and identified multiple binding sites on both proteins.
The N-terminal N-glycan of NEU1 (show NEURL Antibodies) is indispensable for its function, whereas the C-terminal N-glycan appears to be non-essential. The omission of the second N-glycan can be compensated for by upregulating the expression of PPCA
PPGB gene is not responsible for the lysosomal storage disease of Japanese Black cattle.
This gene encodes a glycoprotein which associates with lysosomal enzymes beta-galactosidase and neuraminidase to form a complex of high molecular weight multimers. The formation of this complex provides a protective role for stability and activity. Deficiencies in this gene are linked to multiple forms of galactosialidosis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
lysosomal protective protein
, protective protein for beta-galactosidase
, protective protein for beta-galactosidase (galactosialidosis)
, beta-galactosidase 2
, beta-galactosidase protective protein
, carboxypeptidase C
, carboxypeptidase L
, carboxypeptidase Y-like kininase
, lysosomal carboxypeptidase A
, protective protein cathepsin A
, urinary kininase