Recombinant Mouse Meprin A subunit beta (Mep1b), partial

Code CSB-YP730755MO
MSDS
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Source Yeast
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Code CSB-EP730755MO
MSDS
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Source E.coli
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Code CSB-EP730755MO-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP730755MO
MSDS
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Source Baculovirus
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Code CSB-MP730755MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Mep1b
Uniprot No.
Alternative Names
Mep1b; Mep-1b; Meprin A subunit beta; EC 3.4.24.63; Endopeptidase-2; Meprin B
Species
Mus musculus (Mouse)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. 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.
Gene References into Functions
  1. Results provide evidence that meprin beta is involved in collagen deposition in vivo in the lung of bleomycin treated mice and it localized in region with immature collagen. This suggests that meprin beta can favor the progression of the fibrotic process enhancing collagen processing and deposition. PMID: 28059112
  2. This secreted cysteine protease potently converts membrane-bound meprin beta into its active form, impairing meprin beta shedding and its function as a mucus-detaching protease PMID: 29166602
  3. Meprin alphabeta knockout (alphabetaKO) mice and their wild-type (WT) counterparts to streptozotocin-induced type 1 diabetes. The 18-week survival rates were significantly lower for diabetic meprin alphabetaKO mice when compared to those for their wild type counterparts. PMID: 28804725
  4. These studies provide strong evidence for a pathophysiological link between meprin beta and urinary excretion of cleaved nidogen-1 during cisplatin-induced acute kidney injury. PMID: 25957482
  5. Meprin beta is an endogenous zinc-dependent metalloprotease now shown to cleave the N-terminal region of the MUC2 mucin at two specific sites. PMID: 25114233
  6. Suggest role for in meprin-beta-Fra2 axis in mediating vascular remodelling in pulmonary hypertension. PMID: 24258247
  7. of the 151 new extracellular substrates identified, it was notable that ADAM10 the constitutive alpha-secretase-is activated by meprin beta through cleavage of the propeptide PMID: 22940918
  8. Processing of APP by meprin beta was subsequently validated using in vitro and in vivo approaches. N-terminal APP fragments of about 11 and 20 kDa were found in human and mouse brain lysates but not in meprin beta(-/-) mouse brain lysates PMID: 21646356
  9. Demonstrate that the metalloprotease meprin beta and gamma-ENaC associate directly through cytoplasmic domains. PMID: 20953144
  10. disruption of the meprin beta allele in mice affects embryonic viability, birth weight, renal gene expression profiles, and the distribution of meprin alpha in kidney and intestine. PMID: 12556482
  11. Meprin beta is expressed by leukocytes in the draining lymph node of the intestine, regardless of the inflammatory status of the animal, and is likely to contribute to leukocyte transmigration events important to intestinal immune responses. PMID: 15034068
  12. Following ischemia-reperfusion the redistribution of active meprin-alpha/beta is a major contributor to renal injury and subsequent inflammation. PMID: 18172000
  13. meprinbeta may play a protective role against the progression of renal injury through the degradation of extracellular matrix and bioactive peptides PMID: 18355876

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Subcellular Location
Cell membrane; Single-pass type I membrane protein. Secreted.
Protein Families
Peptidase M12A family
Tissue Specificity
Isoform 1 is expressed in kidney, intestinal brush borders, and salivary ducts. Isoform 2 has been found in carcinoma cells.
Database Links
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7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
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