Mep1b (GeneName), Meprin A subunit beta (ProteinName), MEP1B_MOUSE.
Mouse Mep1b/ Meprin A subunit beta ELISA Kit
Endopeptidase-2, Meprin B, Mep-1b
Natural and recombinant mouse Meprin A subunit beta
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
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.
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.
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.
MDARHQPWFL | VFATFLLVSG | LPAPEKFVKD | IDGGIDQDIF | DINQGLGLDL |
FEGDIKLEAN | GKNSIIGDHK | RWPHTIPYVL | EDSLEMNAKG | VILNAFERYR |
LKTCIDFKPW | SGEANYISVF | KGSGCWSSVG | NIHAGKQELS | IGTNCDRIAT |
VQHEFLHALG | FWHEQSRADR | DDYVIIVWDR | IQPGKEHNFN | IYNDSVSDSL |
NVPYDYTSVM | HYSKTAFQNG | TESTIVTRIS | EFEDVIGQRM | DFSDYDLLKL |
NQLYNCTSSL | SFMDSCDFEL | ENICGMIQSS | GDSADWQRVS | QVLSGPESDH |
SKMGQCKDSG | FFMHFNTSIL | NEGATAMLES | RLLYPKRGFQ | CLEFYLYNSG |
SGNDQLNIYT | REYTTGQQGG | VLTLQRQIKE | VPIGSWQLHY | VTLQVTKKFR |
VVFEGLRGPG | TSSGGLSIDD | INLSETRCPH | HIWHIQNFTQ | ILGGQDTSVY |
SPPFYSSKGY | AFQIYMDLRS | STNVGIYFHL | ISGANDDQLQ | WPCPWQQATM |
TLLDQNPDIR | QRMFNQRSIT | TDPTMTSDNG | SYFWDRPSKV | GVTDVFPNGT |
QFSRGIGYGT | TVFITRERLK | SREFIKGDDI | YILLTVEDIS | HLNSTSAVPD |
PVPTLAVHNA | CSEVVCQNGG | ICVVQDGRAE | CKCPAGEDWW | YMGKRCEKRG |
STRDTVIIAV | SSTVTVFAVM | LIITLVSVYC | TRRKYRKKAR | ANTAAMTLEN |
This product has not yet been referenced specifically in any publications.
"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."
"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."
"The structural genes, MEP1A and MEP1B, for the alpha and beta subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively."
"The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin?β and ADAM10."
"Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane."
"Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading."
"Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score."
"Fetuin-A and cystatin C are endogenous inhibitors of human meprin metalloproteases."
"The metalloprotease meprinbeta processes E-cadherin and weakens intercellular adhesion."
"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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