M5177
Anti-Matrix Metalloproteinase-9, C-Terminal antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-MMP-9
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About This Item
MDL number:
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous glycerol solution
species reactivity
human
concentration
~1 mg/mL
technique(s)
western blot: 1:1,000 using concentrated cell culture medium from a stimulated human cell line (M2928)
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... MMP9(4318)
General description
Matrix metalloproteinase-9 (MMP-9) is a zinc-dependent proteinase which is also known as 92kDa gelatinase-B. It is expressed by various cells like granulocytes and mononuclear cells. The gene encoding it is localized on human chromosome 20q11.2-q13.1 and has 13 exons.
Immunogen
synthetic peptide corresponding to the C-terminal end of human matrix metalloproteinase-9 (gelatinase-B).
Biochem/physiol Actions
By immunoblotting against the reduced protein, the antibody reacts with bands at 92 kDa and 88 kDa (the pro-form and active form). The antibody performs best on reduced proteins, but will react with non-reduced MMP-9. When used on reduced samples from tissue culture media, the antibody also recognizes a band at 65 kDa, which may be removed by enriching the gelatinase on gelatin-agarose.
Matrix metalloproteinase-9 (MMP-9) has been studied as a biomarker of nervous tissue inflammation in multiple sclerosis (MS).
Physical form
Solution in phosphate buffered saline, pH 7.4, containing 50% glycerol and 0.05% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Vishnu C Ramani et al.
Biochimica et biophysica acta, 1813(8), 1525-1531 (2011-05-28)
The gelatinases, matrix metalloproteinase (MMP)-9 and -2, are produced as latent, inactive enzymes that can be proteolytically activated by a number of proteases. In many normal and pathological conditions, where the expression of MMPs is deregulated, changes in the expression
Senem Maral et al.
Medicine, 94(16), e732-e732 (2015-04-24)
Chronic myeloproliferative disorders such as polycythemia vera (PV), essential thrombocytosis (ET), and idiopathic myelofibrosis arise from clonal proliferation of neoplastic stem cells in the bone marrow. Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that have potential to degrade
Xiaoli Zhang et al.
Medical science monitor : international medical journal of experimental and clinical research, 21, 1115-1123 (2015-04-22)
The role of matrix metalloproteinase 9 (MMP-9) polymorphisms in breast cancer risk remains unclear. The purpose of this study was to evaluate the association between MMP-9 variants and breast cancer susceptibility. Case-control studies were searched on electronic databases to retrieve
Tereza C Cardoso et al.
Diagnostic pathology, 5, 57-57 (2010-09-14)
Meningoencephalitis by Herpesvirus type 5 (BoHV-5) in cattle has some features that are similar to those of herpetic encephalitis in humans and other animal species. Human Herpesvirus 3 (commonly known as Varicella-zoster virus 1), herpes simplex viruses (HSV), and equid
Y Benesová et al.
Multiple sclerosis (Houndmills, Basingstoke, England), 15(3), 316-322 (2009-01-21)
Matrix metalloproteinases are notable contributors to neuroinflammation and blood-brain barrier disruption in multiple sclerosis (MS). The goal of this study was to determine the serum levels of matrix metalloproteinase-9 (MMP-9), matrix metalloproteinase-2 (MMP-2), and their tissue inhibitors (TIMP-1) and (TIMP-2)
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