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Meprins are multidomain zinc metalloproteases that are highly expressed in mammalian kidney and intestinal brush border membranes, and in leukocytes and certain cancer cells. Additionally we are shipping Meprin B Kits (13) and Meprin B Proteins (8) and many more products for this protein.
Showing 10 out of 13 products:
no significant dentin malformation was observed in Mep1b (-/-) or Mep1a (show MEP1A Antibodies) (-/-) deficient mice.
meprin alpha (show MEP1A Antibodies) and meprin beta join the modulators of Reelin (show RELN Antibodies) signalling as they cleave Reelin (show RELN Antibodies) at a specific site and are upregulated under specific pathological conditions.
These studies provide strong evidence for a pathophysiological link between meprin beta and urinary excretion of cleaved nidogen-1 (show NID1 Antibodies) during cisplatin-induced acute kidney injury.
While meprin A only cleaved protein kinase A (PKA) catalytic subunit beta1, meprin B cleaved all three PKA catalytic isoforms.
Meprin beta is an endogenous zinc-dependent metalloprotease (show ADAMTS7 Antibodies) now shown to cleave the N-terminal region of the MUC2 (show MUC2 Antibodies) mucin (show SLC13A2 Antibodies) at two specific sites.
Suggest role for in meprin-beta-Fra2 (show FOSL2 Antibodies) axis in mediating vascular remodelling in pulmonary hypertension.
meprin alpha (show MEP1A Antibodies) and meprin beta are unique in their ability to process and release both C- and N-propeptides from type I procollagen (show COL1A2 Antibodies) in vitro and in vivo
of the 151 new extracellular substrates identified, it was notable that ADAM10 (show ADAM10 Antibodies) the constitutive alpha-secretase-is activated by meprin beta through cleavage of the propeptide
the binding of S-MBP to meprins triggers the complement activation through the lectin pathway and may cause the acute renal failure due to ischemia/reperfusion injury on kidney transplantation and hemorrhagic shock
Processing of APP (show APP Antibodies) by meprin beta was subsequently validated using in vitro and in vivo approaches. N-terminal APP (show APP Antibodies) fragments of about 11 and 20 kDa were found in human and mouse brain lysates but not in meprin beta(-/-) mouse brain lysates
TSPAN8 (show TSPAN8 Antibodies) might be important for the orchestration of meprin beta at the cell surface with impact on certain proteolytic processes
n conclusion, we show that the concept of cleavable linkers specific for meprin beta is feasible, as the peptides are rapidly cleaved by the enzyme while retaining their biological properties
Meprin Beta was found to be activated at the cell surface by matriptase-2 (show TMPRSS6 Antibodies).
promotes inflammation in macrophages via ADAM-10 (show ADAM10 Antibodies) dependent pathway
Overexpression of MEP1B is associated with pancreatic neuroendocrine tumors.
Meprin metalloproteases A and B inactivate interleukin 6 (show IL6 Antibodies)
metalloprotease meprin beta generates amino terminal-truncated amyloid beta peptide species
Meprins are multidomain zinc metalloproteases that are highly expressed in mammalian kidney and intestinal brush border membranes, and in leukocytes and certain cancer cells. They are involved in the hydrolysis of a variety of peptide and protein substrates, and have been implicated in cancer and intestinal inflammation. Mature meprins are oligomers of evolutionarily related, but separately encoded alpha and/or beta subunits. Homooligomers of alpha subunit are secreted, whereas, oligomers containing the beta subunit are plasma membrane-bound. This gene encodes the beta subunit. Targeted disruption of this gene in mice affects embryonic viability, renal gene expression profiles, and distribution of the membrane-associated alpha subunit in kidney and intestine.
meprin A, beta
, N-benzoyl-L-tyrosyl-p-amino-benzoic acid hydrolase beta
, meprin A subunit beta
, meprin A subunit beta-like
, meprin B
, meprin beta
, meprin A beta
, N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit beta
, N-benzoyl-L-tyrosyl-p-amino-benzoic acid hydrolase beta subunit
, PABA peptide hydrolase
, PPH beta