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

Details for Product anti-MMP9 Antibody No. ABIN1027712, Supplier: Log in to see
Antigen
  • 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
  • matrix metalloproteinase-9
  • collagenase
  • Matrix metalloproteinase-9
  • matrix metallopeptidase 9
  • matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
  • matrix metalloproteinase 9
  • mmp-9
  • RB3913
  • BPSS0666
  • Sbal_3732
  • Shew_1685
  • Shew_3732
  • Bcer98_0486
  • Shew185_0630
  • Spea_0035
  • Spea_2754
  • Spea_2966
  • Sbal195_0657
  • BcerKBAB4_5655
  • BcerKBAB4_0468
  • BcerKBAB4_2821
  • BcerKBAB4_3229
  • Shal_3056
  • Swoo_0042
  • Swoo_0648
  • Swoo_3449
  • Lbys_3550
  • Palpr_2084
  • mmp9
  • Mmp9
  • MMP9
Alternatives
anti-Rat (Rattus) MMP 9 antibody for Immunoprecipitation
Epitope
AA 1-708
82
43
26
23
15
15
15
11
9
8
8
7
7
6
5
5
5
5
4
4
3
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Human, Mouse (Murine), Rat (Rattus)
468
159
128
21
21
18
10
8
5
4
4
3
3
2
2
2
1
1
1
1
1
Host
Mouse
292
239
6
2
1
Clonality (Clone)
Monoclonal ()
Conjugate
This MMP 9 antibody is un-conjugated
22
18
15
9
6
6
6
6
5
4
4
4
4
4
4
3
3
3
3
3
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
2
1
1
1
Application
Flow Cytometry (FACS), Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blotting (WB)
402
213
206
155
89
68
46
41
37
26
8
8
4
2
2
1
1
1
1
Options
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Immunogen Fusion protein amino acids 1-708 (full length) of rat MMP9
Clone S51-82
Isotype IgG2a
Specificity Detecs ~92 kDa and ~82 kDa (pro and active forms).
Purification Protein G Purified
Alternative Name MMP9 (MMP9 Antibody Abstract)
Background 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 (1). 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 (2-4). MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). 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 (5).
Gene ID 81687
NCBI Accession NP_112317
UniProt P50282
Research Area Cardiovascular, Atherosclerosis, Proteolysis / Ubiquitin, Metalloprotease, Angiogenesis, Extracellular Matrix, Matrix Metalloproteinases
Pathways Cellular Response to Molecule of Bacterial Origin, Positive Regulation of Immune Effector Process
Application Notes
  • WB (1:1000)
  • ICC/IF (1:100)
  • optimal dilutions for assays should be determined by the user.
Comment

1 μg/ml of SMC-396 was sufficient for detection of MMP9 in 20 μg of COS-1 cells (lysate) transfected with human MMP9 by colorimetric immunoblot analysis using goat anti-mouse IgG:HRP as the secondary antibody.

Restrictions For Research Use only
Format Liquid
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 Hirose, Chiba, Karasugi, Nakajima, Kawaguchi, Mikami, Furuichi, Mio, Miyake, Miyamoto, Ozaki, Takahashi, Mizuta, Kubo, Kimura, Tanaka, Toyama, Ikegawa: "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).

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).

Sternlicht, Lochter, Sympson, Huey, Rougier, Gray, Pinkel, Bissell, Werb: "The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis." in: Cell, Vol. 98, Issue 2, pp. 137-46, 1999 (PubMed).

Vu, Shipley, Bergers, Berger, Helms, Hanahan, Shapiro, Senior, Werb: "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).

Nagase, Enghild, Suzuki, Salvesen: "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).