Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase) (MMP9) (AA 1-708) antibody

Details for Product No. ABIN1027712
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Antigen
Synonyms mmp-9, fgMMP-9, mmp9, AW743869, B/MMP9, Clg4b, MMP-9, pro-MMP-9, CLG4B, GELB, MANDP2, clg4b, gelb, mandp2, ZFMMP-9, wu:fb02g06, wu:fb07b05, wu:fi98c09, wu:fj05a08, zgc:64165
Epitope
AA 1-708
(39), (22), (14), (13), (8), (7), (6), (4), (3), (3), (3), (3), (3), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human, Rat (Rattus)
(287), (99), (69), (36), (36), (19), (14), (12), (4), (2), (2), (1), (1), (1), (1)
Host
Mouse
(221), (109), (7)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(15), (10), (9), (4), (4), (4), (4), (4), (4), (4), (4), (3), (3), (3), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Immunohistochemistry (IHC), Western Blotting (WB), Immunoprecipitation (IP)
(232), (101), (87), (86), (62), (38), (35), (24), (21), (15), (2), (2), (1), (1), (1)
Pubmed 5 references available
Quantity 100 µg
Options
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Catalog No. ABIN1027712
367.40 $
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Immunogen Fusion protein AA 1-708 (full length) of rat MMP9
Clone S51-82
Isotype IgG2a
Specificity Detecs approx. 92 kDa and approx. 82 kDa (pro and active forms)
Purification Protein G Purified
Alternative Name MMP9
Background Synonyms:
CLG4B, 82 kDa matrix metalloproteinase-9, collagenease type 4 beta, GELB , Macrophage gelatinase, MANDP2, Type V collagenase
MMP9, otherwise known as matrix metalloproteinase 9, is 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 like arthritis and metastasis. Among the family members, MMP-2, MMP-3, MMP-7 and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis and apoptosis. MMP activity correlates with cancer development. One mechanism of MMP regulation is transcriptional. Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein.
Gene ID 81687
NCBI Accession NP_112317
UniProt P50282
Research Area Cardiovascular, Atherosclerosis, Proteolysis / Ubiquitin, Metalloprotease, Angiogenesis, Extracellular Matrix, Matrix Metalloproteinases, Ion Channels, Transporters
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Background publications Nagase, Enghild, Suzuki et al.: "Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate." in: Biochemistry, Vol. 29, Issue 24, pp. 5783-9, 1990 (PubMed).

Vu, Shipley, Bergers et al.: "MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes." in: Cell, Vol. 93, Issue 3, pp. 411-22, 1998 (PubMed).

Sternlicht, Lochter, Sympson et al.: "The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis." in: Cell, Vol. 98, Issue 2, pp. 137-46, 1999 (PubMed).

Coussens, Fingleton, Matrisian: "Matrix metalloproteinase inhibitors and cancer: trials and tribulations." in: Science (New York, N.Y.), Vol. 295, Issue 5564, pp. 2387-92, 2002 (PubMed).

Hirose, Chiba, Karasugi et al.: "A functional polymorphism in THBS2 that affects alternative splicing and MMP binding is associated with lumbar-disc herniation." in: American journal of human genetics, Vol. 82, Issue 5, pp. 1122-9, 2008 (PubMed).

Validation Images
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