Rat Matrix Metalloproteinase 9 (MMP-9) Protein (Active)

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Description
Rat MMP-9 Protein is a recombinant protein from Rat produced in HEK293 Cells. A DNA sequence encoding the rat MMP9 (EDL96479.1) (Met 1-Pro 708) was expressed, fused with a polyhistidine tag at the C-terminus.
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Product specifications
Category | Proteins and Peptides |
Immunogen Target | MMP-9 |
Host | HEK293 cells |
Origin | Rat |
Observed MW | Molecular Weight: 77.8 kDa Sequence Fragment: Met1-Pro708 Tag: C-terminal His tag Validity: The validity for this protein is 12 months. |
Expression | Recombinant |
Purity | > 95% (SDS-PAGE) |
Size 1 | 50 µg |
Form | |
Tested Applications | SDS-PAGE |
Buffer | Lyophilized from sterile 50mM MES, 100mM NaCl, 1mM CaCl2, 10% Glycerol, pH 7.4. |
Availability | Shipped within 5-15 working days. |
Storage | Aliquot and store at -20°C or -80°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
NCBI Accession | EDL96479.1 |
Alias | GELB,CLG4B,MMP-9,MANDP2,92 kDa type IV collagenase, Gelatinase B |
Background | Protein MMP9 |
Status | RUO |
Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
Matrix metalloproteinase 9 (MMP9), also known as gelatinase B, is an enzyme belonging to the matrix metalloproteinase family. MMP-9 is a zinc-dependent endopeptidase. It is synthesized as a proenzyme, and requires activation by other proteases to become active. The active form of MMP-9 can degrade various components of the extracellular matrix, including collagen type IV, which is a major component of the basement membrane. MMP-9 is implicated in several physiological and pathological processes, including tissue remodeling, angiogenesis, wound healing, inflammation, and cancer metastasis. It is involved in the breakdown of the extracellular matrix, which is essential for processes like tissue repair and remodeling. However, dysregulation of MMP-9 activity can contribute to pathological conditions such as excessive tissue degradation, tumor invasion, and metastasis.MMP-9 activity is tightly regulated at multiple levels, including transcriptional regulation, post-translational modification, and inhibition by tissue inhibitors of metalloproteinases (TIMPs)
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