Matrix Metallopeptidase 7 (Matrilysin, Uterine) (MMP7) Peptide
-
- Target See all MMP7 products
- MMP7 (Matrix Metallopeptidase 7 (Matrilysin, Uterine) (MMP7))
- Origin
- Human
-
Source
- Synthetic
- Application
- Blocking Peptide (BP), Western Blotting (WB)
- Characteristics
- This is a synthetic peptide designed for use in combination with anti-MMP7 antibody (Catalog #: ARP46075_T100). It may block above mentioned antibody from binding to its target protein in western blot and/or immunohistochecmistry under proper experimental settings. There is no guarantee for its use in other applications.
- Purification
- Purified
-
-
- Application Notes
- Each Investigator should determine their own optimal working dilution for specific applications.
- Restrictions
- For Research Use only
-
- Format
- Lyophilized
- Reconstitution
- Add 100 μL of sterile PBS. Final peptide concentration is 1 mg/mL in PBS.
- Concentration
- 1 mg/mL
- Buffer
- Final peptide concentration is 1 mg/mL in PBS.
- Handling Advice
- Avoid repeated freeze-thaw cycles.
- Storage
- -20 °C
- Storage Comment
- For longer periods of storage, store at -20°C. Avoid repeat freeze-thaw cycles.
-
- Target
- MMP7 (Matrix Metallopeptidase 7 (Matrilysin, Uterine) (MMP7))
- Synonyms
- MAT Peptide, MPMM Peptide, MMP-7 Peptide, MPSL1 Peptide, PUMP-1 Peptide, matrilysin Peptide, LOC727698 Peptide, MMP7 Peptide, Matrilysin Peptide, matrix metallopeptidase 7 Peptide, MMP7 Peptide, Mmp7 Peptide
- Background
-
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP7 degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa.Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.
Alias Symbols: MMP-7, MPSL1, PUMP-1
Protein Interaction Partner: ZBTB33,BCAN,CD151,CD44,DCN,FASLG,HAPLN1,HBEGF,MBP,MMP1,MMP9,NGF,PLG,SERPINA1,SPP1,TFPI,TNFSF11,BCAN,CD44,FASLG,HBEGF
Protein Size: 267 - Molecular Weight
- 19 kDa
- Gene ID
- 4316
- NCBI Accession
- NM_002423, NP_002414
- UniProt
- P09237
-