MEP1B Mouse

Meprin A Beta Mouse Recombinant
Cat. No.
BT24039
Source
Sf9 Insect cells.
Synonyms
Meprin A subunit beta (EC:3.4.24.63), Endopeptidase-2, Meprin B, Mep1b, Mep-1b.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

MEP1B produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 642 amino acids (21-654aa) and having a molecular mass of 72.6kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).
MEP1Bis expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Meprin A subunit beta (MEP1B), a member of the astacin family of zinc endopeptidases 1, 2, is a disulfide-linked, tetrameric metalloendopeptidase found in renal brush border membranes. MEP1B is a highly regulated, secreted cell-surface metalloendopeptidase with significant expression in the kidney and intestine.
Description
Produced in Sf9 Insect cells, MEP1B is a single, glycosylated polypeptide chain comprising 642 amino acids (21-654aa) with a molecular weight of 72.6kDa. It's important to note that the molecular size on SDS-PAGE will appear approximately between 70-100kDa. The protein is expressed with an 8 amino acid His tag at the C-Terminus and purified using proprietary chromatographic techniques.
Physical Appearance
The product is a sterile filtered solution, colorless in appearance.
Formulation
The MEP1B protein solution is provided at a concentration of 0.25mg/ml. It is formulated in Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep the vial at 4°C. For longer storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. To maintain protein integrity, avoid repeated freeze-thaw cycles.
Purity
The purity of MEP1B is determined by SDS-PAGE analysis and is greater than 90.0%.
Synonyms
Meprin A subunit beta (EC:3.4.24.63), Endopeptidase-2, Meprin B, Mep1b, Mep-1b.
Source
Sf9 Insect cells.
Amino Acid Sequence
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 STRDVEHHHH HH.

Product Science Overview

Structure and Expression

Meprin β is a membrane-bound metalloprotease that forms disulfide-linked homo- or heterooligomers with meprin α subunits . The recombinant mouse meprin β protein is typically expressed in baculovirus systems and purified to high levels of purity (>90%) for research purposes . The protein is often tagged with a His tag at the C-terminus to facilitate purification and detection .

Biological Functions

Meprin β exhibits a strong preference for acidic amino acids at the P1’ position and is known to cleave a variety of substrates, including:

  • Fibroblast Growth Factor 19 (FGF19)
  • Vascular Endothelial Growth Factor A (VEGFA)
  • Interleukin-1 Beta (IL1B)
  • Interleukin-18 (IL18)
  • Procollagen I and III
  • E-cadherin
  • Kallikrein-related peptidases (KLK7)
  • Gastrin
  • ADAM10
  • Tenascin-C

The presence of several pro-inflammatory cytokines among its substrates implicates meprin β in inflammation. Additionally, its ability to degrade extracellular matrix components suggests a role in tissue remodeling .

Regulatory Mechanisms

Meprin β is proteolytically activated by trypsin in the intestinal lumen and by kallikrein-related peptidases in other tissues . This activation is crucial for its function in various physiological and pathological processes.

Research Applications

Recombinant mouse meprin β protein is widely used in research to study its role in various biological processes. It is particularly useful in investigating its involvement in inflammation, tissue remodeling, and protein shedding. The recombinant protein is also employed in assays to identify potential inhibitors and to understand its substrate specificity .

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