Rat Matrix Metalloproteinase 9 (MMP9) Protein

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Description
Matrix Metalloproteinase 9 Protein is a recombinant Rat protein expressed in E. coli.
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Product specifications
Category | Proteins and Peptides |
Immunogen Target | Matrix Metalloproteinase 9 (MMP9) |
Host | E. coli |
Origin | Rat |
Conjugation | Unconjugated |
Observed MW | Molecular Weight: Calculated MW: 19.5 kDa Observed MW (SDS-PAGE): 19 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Ala226-Asp391 Tag: N-terminal His tag |
Expression | Recombinant |
Purity | > 90% |
Size 1 | 10 µg |
Size 2 | 50 µg |
Size 3 | 100 µg |
Size 4 | 200 µg |
Size 5 | 500 µg |
Form | Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in 20 mM Tris, 150 mM NaCl, pH 8.0. If a higher concentration is required, the product can be reconstituted directly in 20 mM Tris, 150 mM NaCl, pH 8.0, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex. |
Tested Applications | WB, SDS-PAGE |
Buffer | Prior to lyophilization: 20 mM Tris, 150 mM NaCl, pH 8.0, containing 1 mM EDTA, 1 mM DTT, 0.01% Sarcosyl, 5% Trehalose and Proclin-300. |
Availability | Shipped within 5-7 working days. |
Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
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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