Human Pro-Matrix Metalloproteinase 9 (Pro-MMP-9) Protein
351€ (10 µg)
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935106861
info@markelab.com
name
Human Pro-Matrix Metalloproteinase 9 (Pro-MMP-9) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx682049
tested applications
SDS-PAGE
Description
Human Pro-Matrix Metalloproteinase 9 (Pro-MMP-9) Protein is a recombinant Human protein expressed in E. coli.
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Pro-Matrix Metalloproteinase 9 (Pro-MMP-9) |
| Host | E. coli |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Origin | Human |
| Conjugation | Unconjugated |
| Expression | Recombinant |
| Size 1 | 10 µg |
| Size 2 | 100 µg |
| Size 3 | 1 mg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 10-20 working days. |
| Storage | Aliquot and store at -20 °C. |
| Dry Ice | No |
| UniProt ID | P14780 |
| 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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