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Anti-MMP9 antibody

[STJ24592] Download PDF Print Data Sheet

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Product name Anti-MMP9 antibody
Short Description Rabbit Polyclonal against MMP9 protein
Description The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors and adhesion molecules (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).
Applications IHC, WB
Dilution range WB 1:500-1:2000
IHC 1:50-1:200
ICC 1:50-1:200
Protein Name Matrix metalloproteinase-9
92 kDa gelatinase
92 kDa type IV collagenase
Gelatinase B
67 kDa matrix metalloproteinase-9
82 kDa matrix metalloproteinase-9
Immunogen A synthetic peptide derived from human MMP9.
Storage Instruction Store at -20°C, and avoid repeat freeze-thaw cycles.
Note For Research Use Only (RUO).
Host Rabbit
Clonality Polyclonal
Reactivity Human, Mouse
Conjugation Unconjugated
Concentration 1 mg/ml
Purification Anti-MMP9 antibody was affinity purified using immunizing peptide
Isotype IgG
Formulation PBS with 0.02% sodium azide, 50% glycerol, pH7.4
Gene ID 4318
Gene Symbol MMP9
Database Links HGNC:7176
Alternative Names MMP9 antibody
CLG4B antibody
Matrix metalloproteinase-9 antibody
MMP-9 antibody
92 kDa gelatinase antibody
92 kDa type IV collagenase antibody
Gelatinase B antibody
GELB antibody
67 kDa matrix metalloproteinase-9 antibody
82 kDa matrix metalloproteinase-9 antibody
Function May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.
Post-translational Modifications Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9. ; N- and O-glycosylated.
Cellular Localization Secreted, extracellular space, extracellular matrix
Tissue Specificity Produced by normal alveolar macrophages and granulocytes.
Sequence and Domain Family The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.


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Shih MF, Pan KH, Cherng JY. Possible Mechanisms of Di(2-ethylhexyl) Phthalate-Induced MMP-2 and MMP-9 Expression in A7r5 Rat Vascular Smooth Muscle Cells. International Journal of Molecular Sciences. 2015. 16, 28800-28811. doi:10.3390/ijms161226131