Matrix Metalloproteinase 9 (MMP9) Protein is a Human protein produced in Yeast (Pichia pastor).
MMPs are secreted by diverse connective tissue and pro-inflammatory cells. Typically, these enzymes exhibit minimal expression under normal physiological circumstances. MMPs assume a pivotal role in various cellular processes, including cell proliferation, migration, differentiation, angiogenesis, apoptosis, and immunity. They share a common domain structure, consisting of three key components. First is the pro-peptide, which requires removal to activate the enzyme. Next, there is the catalytic domain, featuring a cysteine switch, where a cysteine residue interacts with zinc, and the haemopexin-like C-terminal domain is linked to the catalytic domain via a flexible hinge region. MMP-9, alternatively known as 92 kDa type IV collagenase, 92 kDa gelatinase, or gelatinase B (GELB), belongs to the zinc-metalloproteinases within the Matrixin family. In humans, the MMP-9 gene is responsible for encoding this enzyme. MMP-9's substrates include gelatin and collagen types IV and V. This gelatinase, MMP-9, has been associated with various medical conditions, including the development of atherosclerosis, chronic obstructive pulmonary disease (COPD), tumor formation, metastasis, and wound repair
Proteins and Peptides
Human
Yeast
Matrix Metalloproteinase 9 (MMP9)
Yeast
Unconjugated
Lyophilized
WB, SDS-PAGE
1 mg
5 mg
Recombinant
> 90%
Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.
Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.
MMP9
No
Shipped within 1-2 months.
GELB,CLG4B,MMP-9,MANDP2,92 kDa type IV collagenase, Gelatinase B
This product is for research use only. <p></p> Not for human consumption, cosmetic, therapeutic or diagnostic use.
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