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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. Zusätzlich bieten wir Ihnen Meprin B Antikörper (13) und Meprin B Proteine (8) und viele weitere Produktgruppen zu diesem Protein an.
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no significant dentin malformation was observed in Mep1b (-/-) or Mep1a (zeige MEP1A ELISA Kits) (-/-) deficient mice.
meprin alpha (zeige MEP1A ELISA Kits) and meprin beta join the modulators of Reelin (zeige RELN ELISA Kits) signalling as they cleave Reelin (zeige RELN ELISA Kits) 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 (zeige NID1 ELISA Kits) 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 (zeige ADAMTS7 ELISA Kits) now shown to cleave the N-terminal region of the MUC2 (zeige MUC2 ELISA Kits) mucin (zeige SLC13A2 ELISA Kits) at two specific sites.
Suggest role for in meprin-beta-Fra2 (zeige FOSL2 ELISA Kits) axis in mediating vascular remodelling in pulmonary hypertension.
meprin alpha (zeige MEP1A ELISA Kits) and meprin beta are unique in their ability to process and release both C- and N-propeptides from type I procollagen (zeige COL1A2 ELISA Kits) in vitro and in vivo
of the 151 new extracellular substrates identified, it was notable that ADAM10 (zeige ADAM10 ELISA Kits) 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 (zeige APP ELISA Kits) by meprin beta was subsequently validated using in vitro and in vivo approaches. N-terminal APP (zeige APP ELISA Kits) fragments of about 11 and 20 kDa were found in human and mouse brain lysates but not in meprin beta(-/-) mouse brain lysates
TSPAN8 (zeige TSPAN8 ELISA Kits) 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 (zeige TMPRSS6 ELISA Kits).
promotes inflammation in macrophages via ADAM-10 (zeige ADAM10 ELISA Kits) dependent pathway
Overexpression of MEP1B is associated with pancreatic neuroendocrine tumors.
Meprin metalloproteases A and B inactivate interleukin 6 (zeige IL6 ELISA Kits)
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