Proteins of the matrix metalloproteinase (MMP) family are 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, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
Categories
Primary Antibodies
Clonality
polyclonal
Description
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.
Host
Rabbit
Immunogen
matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
Isotype
IgG
Molecular Weight
68 kDa
Reactivity
Human, Mouse, Rat
Regulatory
RUO
Synonyms
92 kDa gelatinase, 92 kDa type IV collagenase, CLG4B, Gelatinase B, GELB, Matrix metalloproteinase 9, MMP 9, MMP9
Uniprot
P14780
Gene Id
4318
Research Area
Cancer, Cardiovascular, Metabolism
Form
liquid
Format
liquid
Purification
Immunogen affinity purified
Purity
>=95% as determined by SDS-PAGE
Storage
PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20°C for 12 months (Avoid repeated freeze / thaw cycles.)