IM35
Anti-MMP-1 (Ab-1) Mouse mAb (41-1E5)
liquid, clone 41-1E5, Calbiochem®
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Product Name
Anti-MMP-1 (Ab-1) Mouse mAb (41-1E5), liquid, clone 41-1E5, Calbiochem®
biological source
mouse
antibody form
purified antibody
antibody product type
primary antibodies
clone
41-1E5, monoclonal
form
liquid
contains
≤0.1% sodium azide as preservative
species reactivity
human
should not react with
bovine
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
dilution
(Frozen sections
Immunoblotting (1 µg/mL)
Paraffin sections (2.5 µg/mL, pressure cooker pre-treatment required))
isotype
IgG2a
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... MMP1(4312)
Application
Frozen sections (see application references)
Immunoblotting (1 g/ml)
Paraffin sections (2.5 g/ml, pressure cooker pre-treatment required)
Disclaimer
Toxicity: Standard Handling (A)
General description
Matrix metalloproteinases (MMPs) are a family of enzymes that are responsible for the degradation of extracellular matrix components such as collagen, laminin and proteoglycans. In addition to sequence homology, all MMPs share the following characteristics: the catalytic mechanism is dependent upon a zinc ion at the active center, they cleave one or more extracellular matrix components, they are secreted as zymogens which are activated by removal of an ~10 kDa segment from the N-terminus and they are inhibited by tissue inhibitor of metalloproteinases (TIMP). These enzymes are involved in normal physiological processes such as embryogenesis and tissue remodeling and may play an important role in arthritis, periodontitis, and metastasis.MMP-1 (interstitial collagenase, tissue collagenase, fibroblast collagenase) is secreted as a 57/52 kDa zymogen which is proteolytically processed to the 46/42 kDa active forms. This enzyme displays substrate specificity toward type I, II, III, VII, VIII and X collagens and gelatin. MMP-1 is thought to play an important role in pathophysiological degradation processes associated with conditions such as rheumatoid arthritis, osteoarthritis, and cancer cell invasion.
Purified mouse monoclonal antibody. Recognizes the ~55 kDa latent and the ~43 kDa active forms of MMP-1.
Recognizes the ~55 kDa latent and the ~43 kDa active forms of MMP-1.
Immunogen
Human
a synthetic peptide (VQGQNVLHGYPKDIYSSFG) corresponding to amino acids 332-350 of human MMP-1
Legal Information
Manufactured by Daiichi Fine Chemical Co., Ltd. Not available for sale in Japan.
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Other Notes
Cottam, D.W. and Rees, R.C. 1993. Intl. J. Oncol.2, 861.
Stetler-Stevenson, W.G., et al. 1993. FASEB7, 1434.
Zhang, J., et al. 1993. Clinica Chimica Acta.219, 1.
Woessner, J.F. 1991. FASEB5, 2145.
Liotta, L.A. and Stetler-Stevenson, W.G. 1990. in Seminars in Cancer Biology, ed. M. M. Gottesman. Vol. 1; 99-106.
Stetler-Stevenson, W.G., et al. 1993. FASEB7, 1434.
Zhang, J., et al. 1993. Clinica Chimica Acta.219, 1.
Woessner, J.F. 1991. FASEB5, 2145.
Liotta, L.A. and Stetler-Stevenson, W.G. 1990. in Seminars in Cancer Biology, ed. M. M. Gottesman. Vol. 1; 99-106.
To prepare conditioned medium for positive control, incubate HT-1080 cells for 2 h at 37°C in serum-free media containing 100 nM PMA. Collect and centrifuge medium; concentrate as necessary. Does not cross-react with bovine. Will not cross-react with human MMP-2, MMP-3, MMP-8, MMP-9, or MMP-13. For best results with paraffin sections, pre-treat with a pressure cooker; however, heat, saponin or trypsin can be used in place of a pressure cooker. Antibody should be titrated for optimal results in individual systems.
Packaging
Please refer to vial label for lot-specific concentration.
Physical form
In 100 mM sodium phosphate buffer, 0.1% BSA, pH 7.0
Preparation Note
Following initial thaw, aliquot and freeze (-20°C).
Not finding the right product?
Try our Product Selector Tool.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
新产品
This item has
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Jennifer A Dixon et al.
Circulation, 120(11 Suppl), S220-S229 (2009-09-24)
Targeted delivery of mesenchymal precursor cells (MPCs) can modify left ventricular (LV) cellular and extracellular remodeling after myocardial infarction (MI). However, whether and to what degree LV remodeling may be affected by MPC injection post-MI, and whether these effects are
Jennifer A Dixon et al.
Circulation, 124(11 Suppl), S35-S45 (2011-09-23)
Although localized delivery of biocomposite materials, such as calcium hydroxyapatite (CHAM), have been demonstrated to potentially attenuate adverse left ventricular (LV) remodeling after myocardial infarction (MI), the underlying biological mechanisms for this effect remain unclear. This study tested the hypothesis
Patrick Meylan et al.
Scientific reports, 11(1), 7847-7847 (2021-04-14)
The thioredoxin system plays key roles in regulating cancer cell malignancy. Here we identify the Thioredoxin-interacting protein (TXNIP) as a gene, which expression is regulated by PPARγ in melanoma cells. We show that high TXNIP expression levels associate with benign
Francisco Wanderley Garcia Paula-Silva et al.
Journal of endodontics, 36(2), 231-237 (2010-02-02)
The objective of this study was to investigate the expression of matrix metalloproteinases (MMPs) in apical periodontitis and during the periapical healing phase after root canal treatment. Apical periodontitis was induced in dog teeth, and root canal treatment was performed
Margarita Espona-Fiedler et al.
Pharmaceutics, 15(1) (2023-01-22)
Metastasis is the primary cause of death in cancer patients. Many current chemotherapeutic agents only show cytotoxic, but not antimetastatic properties. This leads to a reduction in tumor size, but allows cancer cells to disseminate, which ultimately causes patient death.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service