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Meprin A, beta Proteins (MEP1B)

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 (8) and Meprin B Antibodies (7) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
MEP1B 17288 Q61847
MEP1B 25727 P28826
MEP1B 4225 Q16820
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Top Meprin B Proteins at antibodies-online.com

Showing 7 out of 7 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
Insect Cells Mouse rho-1D4 tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 0.25 mg Log in to see 49 to 54 Days
$4,244.78
Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
Insect Cells Human rho-1D4 tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 0.5 mg Log in to see 49 to 54 Days
$6,041.49
Details
HOST_Escherichia coli (E. coli) Rat His tag,T7 tag 100 μg Log in to see 11 to 13 Days
$844.80
Details
Yeast Rat His tag   1 mg Log in to see 56 to 66 Days
$3,835.33
Details
HOST_Human Cells Human His tag,ECD 50 μg Log in to see 16 Days
$547.80
Details

MEP1B Proteins by Origin and Source

Origin Expressed in Conjugate
Mouse (Murine) ,
,
Rat (Rattus) ,
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Human , ,
, ,

More Proteins for Meprin A, beta (MEP1B) Interaction Partners

Zebrafish Meprin A, beta (MEP1B) interaction partners

Mouse (Murine) Meprin A, beta (MEP1B) interaction partners

  1. meprin alpha (show MEP1A Proteins) and meprin beta join the modulators of Reelin (show RELN Proteins) signalling as they cleave Reelin (show RELN Proteins) at a specific site and are upregulated under specific pathological conditions.

  2. These studies provide strong evidence for a pathophysiological link between meprin beta and urinary excretion of cleaved nidogen-1 (show NID1 Proteins) during cisplatin-induced acute kidney injury.

  3. While meprin A only cleaved protein kinase A (PKA) catalytic subunit beta1, meprin B cleaved all three PKA catalytic isoforms.

  4. Meprin beta is an endogenous zinc-dependent metalloprotease (show ADAMTS7 Proteins) now shown to cleave the N-terminal region of the MUC2 (show MUC2 Proteins) mucin (show SLC13A2 Proteins) at two specific sites.

  5. Suggest role for in meprin-beta-Fra2 (show FOSL2 Proteins) axis in mediating vascular remodelling in pulmonary hypertension.

  6. meprin alpha (show MEP1A Proteins) and meprin beta are unique in their ability to process and release both C- and N-propeptides from type I procollagen (show COL1A2 Proteins) in vitro and in vivo

  7. of the 151 new extracellular substrates identified, it was notable that ADAM10 (show ADAM10 Proteins) the constitutive alpha-secretase-is activated by meprin beta through cleavage of the propeptide

  8. 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

  9. Processing of APP (show APP Proteins) by meprin beta was subsequently validated using in vitro and in vivo approaches. N-terminal APP (show APP Proteins) fragments of about 11 and 20 kDa were found in human and mouse brain lysates but not in meprin beta(-/-) mouse brain lysates

  10. Demonstrate that the metalloprotease (show ADAMTS7 Proteins) meprin beta and gamma-ENaC (show SCNN1G Proteins) associate directly through cytoplasmic domains.

Human Meprin A, beta (MEP1B) interaction partners

  1. 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

  2. Meprin Beta was found to be activated at the cell surface by matriptase-2 (show TMPRSS6 Proteins).

  3. promotes inflammation in macrophages via ADAM-10 (show ADAM10 Proteins) dependent pathway

  4. Overexpression of MEP1B is associated with pancreatic neuroendocrine tumors.

  5. Suggest role for in meprin-beta-Fra2 (show FOSL2 Proteins) axis in mediating vascular remodelling in pulmonary hypertension.

  6. Meprin metalloproteases A and B inactivate interleukin 6 (show IL6 Proteins)

  7. of the 151 new extracellular substrates identified, it was notable that ADAM10 (show ADAM10 Proteins) the constitutive alpha-secretase-is activated by meprin beta through cleavage of the propeptide

  8. metalloprotease (show ADAM8 Proteins) meprin beta generates amino terminal-truncated amyloid beta peptide species

  9. Processing of APP (show APP Proteins) by meprin beta was subsequently validated using in vitro and in vivo approaches. N-terminal APP (show APP Proteins) fragments of about 11 and 20 kDa were found in human and mouse brain lysates but not in meprin beta(-/-) mouse brain lysates

  10. Demonstrate that the metalloprotease (show ADAM8 Proteins) meprin beta and gamma-ENaC (show SCNN1G Proteins) associate directly through cytoplasmic domains.

Meprin B (MEP1B) Protein Profile

Protein Summary

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.

Gene names and symbols associated with Meprin A, beta Proteins (MEP1B)

  • meprin A, beta (MEP1B)
  • meprin A, beta (mep1b)
  • meprin 1 beta (Mep1b)
  • Mep-1b protein
  • MEP1B protein
  • si:ch211-191a24.6 protein
  • zgc:153272 protein

Protein level used designations for Meprin A, beta Proteins (MEP1B)

meprin A, beta , N-benzoyl-L-tyrosyl-p-amino-benzoic acid hydrolase beta , meprin A subunit beta , meprin A subunit beta-like , endopeptidase-2 , 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

GENE ID SPECIES
421097 Gallus gallus
468515 Pan troglodytes
490497 Canis lupus familiaris
540701 Bos taurus
707036 Macaca mulatta
100031050 Monodelphis domestica
100124942 Xenopus (Silurana) tropicalis
100151009 Danio rerio
100406280 Callithrix jacchus
100461703 Pongo abelii
100474827 Ailuropoda melanoleuca
100516141 Sus scrofa
100545010 Meleagris gallopavo
100563868 Anolis carolinensis
100587715 Nomascus leucogenys
17288 Mus musculus
25727 Rattus norvegicus
4225 Homo sapiens
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