Human MMP-8 Antibody Summary
-10, -12, or -13.
Phe21-Gly467
Accession # AAZ38714
Applications
Human MMP-8 Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Human MMP-8 by Western Blot MMP-8 expression in; primary normal and DCIS myoepithelial cells and a cell line model. a Normal and ductal carcinoma in situ (DCIS) tissue immunohistochemically stained for matrix metalloproteinase-8 (MMP-8) (Atlas, HPA02122, 1:1000). Clear MMP-8 staining can be observed in the normal myoepithelial cells (MECs), which is absent in the DCIS section. Magnification × 400. b Normal MECs and luminal epithelial cells (LECs) were isolated from reduction mammoplasty tissue and DCIS MEC and DCIS LEC were isolated from a patient with high-grade DCIS. Tissues were enzymatically digested and magnetic bead separation was used to isolated specific populations (MEC - ITGB4, LEC - EpCAM). RNA was extracted from the isolated cells and G361 cells (a positive control for MMP-8), converted to cDNA by reverse transcription and then subjected to nested PCR for MMP-8 or PCR of housekeeping gene 18S. The MMP-8 PCR produces a product of 150 bp in normal MEC and G361 lanes, and other lanes only give a weak band. 18S gives a size of 52 bp in all sample lanes. The water (H2O) control lane shows no band. c (i) RNA was extracted from cell lines; G361, N-1089 and beta 6-1089 and converted to cDNA as above. The cDNA was subjected to nested PCR for MMP-8 and bands were identified in G361 and N-1089 but only a weak band was observed in the beta 6-1089 lane. All samples demonstrated a band for 18S. (ii) RIPA protein lysates were produced from N-1089 and beta 6-1089 cells and 20 ug of protein was run on 8% PAGE then transferred to nitrocellulose and probed for MMP-8 (R&D Systems, mAb 908) alpha v beta 6 (Santa Cruz Biotechnology, SC-6632) or HSC70 as a loading control. The gel indicates that N-1089 expresses higher levels of MMP-8 and much lower levels of alpha v beta 6. While beta 6-1089 exhibit much higher levels of alpha v beta 6 and lower levels of MMP-8. (iii) Densitometry of western blots indicates that MMP-8 expression in N-1089 is 2.5-fold higher than N-1089 and (iv) alpha v beta 6 expression in beta 6-1089 is 10-fold higher than N-1089 Image collected and cropped by CiteAb from the following publication (https://breast-cancer-research.biomedcentral.com/articles/10.1186/s13058-017-0822-9), licensed under a CC-BY license. Not internally tested by R&D Systems.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: MMP-8
Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP‑8 (neutrophil collagenase) is expressed in neutrophils, where it is stored in specific granules. MMP‑8 release from the neutrophils is stimulated by various factors such as interleukins 1 and 8, TNF-alpha and GM-CSF. MMP‑8 is capable of cleaving types I, II and III triple-helical collagen, gelatin peptides, fibronectin, proteoglycans, aggrecan, serpins, beta -casein and peptides such as angiotensin and substance P. In addition to its function in phagocytosis,
MMP‑8 has a high capacity for infiltrating connective tissue, and is implicated in the breakdown of the extracellular matrix in diseases such as rheumatoid arthritis. Structurally, MMP‑8 consists of several domains: a pro-domain that is cleaved upon activation, a catalytic domain containing the zinc-binding site, a short hinge region and a hemopexin-like domain. MMP‑8 is heavily glycosylated.
Product Datasheets
Citations for Human MMP-8 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 4
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A Prototype Antibody-based Biosensor for Measurement of Salivary MMP-8 in Periodontitis using Surface Acoustic Wave Technology
Authors: John J. Taylor, Katrin M. Jaedicke, Rachel C. van de Merwe, Susan M. Bissett, Nichola Landsdowne, Kerry M. Whall et al.
Scientific Reports
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Concerted actions by MMPs, ADAMTS and serine proteases during remodeling of the cartilage callus into bone during osseointegration of hip implants
Authors: J Cassuto, A Folestad, J Göthlin, H Malchau, J Kärrholm
Bone Rep, 2020-09-11;13(0):100715.
Species: Human
Sample Types: Plasma
Applications: ELISA Capture -
Loss of MMP-8 in ductal carcinoma in situ (DCIS)-associated myoepithelial cells contributes to tumour promotion through altered adhesive and proteolytic function
Authors: M Sarper, MD Allen, J Gomm, L Haywood, J Decock, S Thirkettle, A Ustaoglu, SJ Sarker, J Marshall, DR Edwards, JL Jones
Breast Cancer Res, 2017-03-23;19(1):33.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot -
Matrix metalloprotease-9 dysregulation in lower airway secretions of cystic fibrosis patients.
Authors: Gaggar A, Li Y, Weathington N, Winkler M, Kong M, Jackson P, Blalock JE, Clancy JP
Am. J. Physiol. Lung Cell Mol. Physiol., 2007-03-23;293(1):L96-L104.
Species: Human
Sample Types: Sputum
Applications: Activity Assay
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