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Mep1b (GeneName), Meprin A subunit beta (ProteinName), MEP1B_MOUSE.
Product Name:

Mouse Mep1b/ Meprin A subunit beta ELISA Kit

Cat.#:

E1619m

Brand:
EIAab®
Regulatory Status:
Alternative:

Endopeptidase-2, Meprin B, Mep-1b

Detection Method:
ELISA
Assay Type:
Sandwich
Detection Range:
0.312-20ng/mL
Sensitivity:
0.168ng/mL
Specificity:
Natural and recombinant mouse Meprin A subunit beta
Sample Type:
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Sample Data:
Assay Procedure:
Assay Procedure
Research Area:
-
Mouse Mep1b ELISA Kit
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Mouse Mep1b ELISA Kit
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Product Datasheets
Instruction: Down Instruction
MSDS: MSDS


General Annotation


Sub Unit:
Homotetramer consisting of disulfide-linked beta subunits, or heterotetramer of two alpha and two beta subunits formed by non-covalent association of two disulfide-linked heterodimers. Interacts with MBL2 through its carbohydrate moiety. This interaction may inhibit its catalytic activity.


Function:
Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position (PubMed:11278902). Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components.


Subcellular Location:
Cell membrane Single-pass type I membrane protein Secreted Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17.


This product has not yet been referenced specifically in any publications.

[1].
"Human meprin beta: O-linked glycans in the intervening region of the type I membrane protein protect the C-terminal region from proteolytic cleavage and diminish its secretion."

[2].
"Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells."

[3].
"The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively."

[4].
"The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin?β and ADAM10."

[5].
"Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane."

[6].
"Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading."

[7].
"Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score."

[8].
"Fetuin-A and cystatin C are endogenous inhibitors of human meprin metalloproteases."

[9].
"The metalloprotease meprinbeta processes E-cadherin and weakens intercellular adhesion."

[10].
"The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation."
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