Recombinant Human MMP9 protein (His Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

His Tag

Activity

not tested

Cat no : Eg0442

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Validation Data Gallery

• 

  Purity of Recombinant Human MMP9 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

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Product Information

• Purity: >90 %, SDS-PAGE
• Endotoxin: <0.1 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Human MMP9 protein Ala20-Asp707 (Accession# P14780) with a His tag at the C-terminus.
• GeneID: 4318
• Accession: P14780
• PredictedSize: 80.1 kDa
• SDS-PAGE: 80-100 kDa, reducing (R) conditions
• Formulation: Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

MMP9 (matrix metallopeptidase 9), also named as Gelatinase B, is a member of matrix metalloproteinase (MMP) family. The MMP family of enzymes is comprised of critically important extracellular matrix remodeling proteases whose activity has been implicated in normal embryogenesis, tissue remodelling and many diseases such as arthritis, cancer, periodontitis, glomerulonephritis, encephalomyelitis, atherosclerosis and tissue ulceration. MMP9 is produced by a variety of normal and transformed cells including neutrophils, monocytes, macrophages, astrocytes, fbroblasts, osteoclasts and so on. Transgenic mouse models report that MMP9 contributes to skin carcinogenesis, suppresses development of experimental abdominal aortic aneurysms, and triggers the angiogenic switch during carcinogenesis.

References:

1. Roy, Roopali. et al. (2009) J Clin Oncol. 27(31):5287-5297. 
2. Tanindi, Asli. et al. (2011) Open Cardiovasc Med J. 5:110-116. 
3. Coussens, L M. et al. (2000) Cell. 103(3):481-490. 
4. Pyo, R. et al. (2000) J Clin Invest. 105(11):1641-1649. 
5.Bergers, G. et al. (2000) Nat Cell Biol. 2(10):737-744.