protein

Recombinant Human ProMatrix Metalloproteinase-9

MBS143694

0.01 mg

205 USD

Recombinant Protein

Recombinant Human ProMatrix Metalloproteinase-9

ProMatrix Metalloproteinase-9

ProMMP 9 Human; Pro-Matrix Metalloproteinase-9 Human Recombinant; Matrix metalloproteinase-9; MMP-9; 92 kDa type IV collagenase; 92 kDa gelatinase; Gelatinase B; GELB; MMP9; CLG4B

matrix metalloproteinase-9 preproprotein; Matrix metalloproteinase-9; matrix metalloproteinase-9; macrophage gelatinase; matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); type V collagenase; matrix metallopeptidase 9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; GELB

ProMMP 9

MMP9; MMP9; GELB; CLG4B; MMP-9; MANDP2; CLG4B; MMP-9; GELB

MMP9_HUMAN

E Coli

707

Greater than 95.0% as determined by SDS-PAGE.

Pro-MMP-9 protein is supplied in 1x PBS and 50% glycerol. Sterile Filtered clear solution.

Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. Please avoid freeze thaw cycles.

ENZYMES; Enzymes; Matrix Metalloproteinase

Description: Pro-MMP-9 Human Recombinant produced in E Coli is single, a non-glycosylated, Polypeptide chain containing 688 amino acids fragment (20-707) corresponding to the pro form of the protein minus the signal peptide, having a total molecular mass of 78.59kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Pro-MMP-9 is purified by proprietary chromatographic techniques. Introduction: Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).

74272287

NP_004985.2

NM_004994.2

P14780

78,458 Da

AGE/RAGE Pathway 698754!!Activation Of Matrix Metalloproteinases Pathway 576264!!Angiogenesis Pathway 198772!!Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway 730306!!Axon Guidance Pathway 105688!!Bladder Cancer Pathway 83115!!Bladder Cancer Pathway 527!!CXCR4-mediated Signaling Events Pathway 137910!!Collagen Degradation Pathway 730309!!Collagen Formation Pathway 645288

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. [provided by RefSeq, Jul 2008]

0.01 mg

205 USD