IM32
Anti-TIMP-1 (Ab-1) Mouse mAb (7-6C1)
liquid, clone 7-6C1, Calbiochem®
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
Product Name
Anti-TIMP-1 (Ab-1) Mouse mAb (7-6C1), liquid, clone 7-6C1, Calbiochem®
biological source
mouse
antibody form
purified antibody
antibody product type
primary antibodies
clone
7-6C1, monoclonal
form
liquid
contains
≤0.1% sodium azide as preservative
species reactivity
rat, bovine, human
should not react with
mouse
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
dilution
(Immunoblotting (1 µg/mL,
Immunocytochemistry
Paraffin Sections (25 µg/mLs))
isotype
IgG1
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... TIMP1(7076)
Analysis Note
Positive Control
rTIMP-1 Protein (Cat. Nos. PF019 or PF020)
rTIMP-1 Protein (Cat. Nos. PF019 or PF020)
Application
Immunoblotting (1 g/ml, see application references)
Immunocytochemistry (see application references)
Paraffin Sections (25 g/ml, see application references, see comments)
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 approximately 10 kDa segment from the N-terminus and their activity is regulated by endogenous inhibitors. 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.The activation and activity of MMPs are regulated by a family of endogenous inhibitors, tissue inhibitors of metalloproteinase (TIMP). TIMP-1 (also called EPA, Fibroblast collagenase inhibitor or collagenase inhibitor) is a 28 kDa glycoprotein that is expressed by a variety of cell types. It forms a non-covalent, stoichiometric complex with both latent and active MMPs. TIMP-1 preferentially binds and inhibits MMP-9. TIMPs are capable of altering the metastatic potential of cancer cells and have been shown to inhibit invasion and metastasis in animal models.
Purified mouse monoclonal antibody (see application references). Recognizes the ~28 kDa TIMP-1 protein.
Recognizes the ~28.5 kDa TIMP-1 protein. Also recognizes MMP/TIMP-1 complexes.
This Anti-TIMP-1 (Ab-1) Mouse mAb (7-6C1) is validated for use in Immunoblotting, Immunocytochemistry, Paraffin Sections for the detection of TIMP-1 (Ab-1).
Immunogen
Bovine
purified, bovine dental pulp TIMP-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
Also recognizes TIMP-1/MMP complexes.This antibody has been used to stain paraffin sections fixed with PLP (perioddate-lysine-4% paraformaldehyde) and 10% formaldehyde (using 25 µg/ml antibody). Antibody should be titrated for optimal results in individual systems.
Fujimoto, N. and Iwata, K., 1994. Connective Tissue26, 237.
Cottam, D. W. and Rees, R. C., 1993. Intl. J. Oncol.2, 861.
Stetler-Stevenson, W. G., et al. 1993. FASEB J.7, 1434.
Woessner, J. F., 1991. FASEB J.5, 2145.
Liotta, L. A. and Stetler-Stevenson, W. G. 1990. in Seminars in Cancer Biology ed. M. M. Gottesman. Vol. 99-106.
Cottam, D. W. and Rees, R. C., 1993. Intl. J. Oncol.2, 861.
Stetler-Stevenson, W. G., et al. 1993. FASEB J.7, 1434.
Woessner, J. F., 1991. FASEB J.5, 2145.
Liotta, L. A. and Stetler-Stevenson, W. G. 1990. in Seminars in Cancer Biology ed. M. M. Gottesman. Vol. 99-106.
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).
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Storage Class
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
does not flash
flash_point_c
does not flash
Regulatory Information
新产品
This item has
Certificates of Analysis (COA)
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S M Cork et al.
Oncogene, 31(50), 5144-5152 (2012-02-15)
Brain-specific angiogenesis inhibitor 1 (BAI1), an orphan G protein-coupled receptor-type seven transmembrane protein, was recently found mutated or silenced in multiple human cancers and can interfere with tumor growth when overexpressed. Yet, little is known about its regulation and the
Mengli Chen et al.
Journal of ethnopharmacology, 143(2), 448-454 (2012-07-17)
Cordyceps sinensis is a fungus used in traditional Chinese medicine as a tonic to soothe the lung for the treatment of fatigue and respiratory diseases. Idiopathic pulmonary fibrosis is a chronic, irreversible and debilitating lung disease showing fibroblast/myofibroblast expansion and
Georgina González-Avila et al.
Experimental and therapeutic medicine, 12(3), 1419-1427 (2016-09-08)
Asthma airway remodeling is characterized by the thickening of the basement membrane (BM) due to an increase in extracellular matrix (ECM) deposition, which contributes to the irreversibility of airflow obstruction. Interstitial collagens are the primary ECM components to be increased
Susan Notohamiprodjo et al.
Biological chemistry, 393(12), 1463-1470 (2013-05-15)
Tissue inhibitor of metalloproteinase 1 (TIMP-1) controls matrix metalloproteinase activity through 1:1stoichiometric binding. Human TIMP-1 fused to a glycosylphosphatidylinositol(GPI) anchor (TIMP-1 - GPI) shifts the activity of TIMP-1 from the extracellular matrix to the cell surface. TIMP-1 - GPI treated
Hsueh-Liang Fu et al.
The Journal of biological chemistry, 288(17), 12114-12129 (2013-03-23)
The discoidin domain receptors (DDRs) are receptor tyrosine kinases that upon binding to collagens undergo receptor phosphorylation, which in turn activates signal transduction pathways that regulate cell-collagen interactions. We report here that collagen-dependent DDR1 activation is partly regulated by the
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