Protein

MMP-9 (Catalytic Domain), human recombinant

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  • Cat.Number : AS-55576-1
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    In stock
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Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-9 (92-kDa gelatinase, collagenase-IV) is involved in a number of diseases such as cancer, angiogenesis, alopecia, and metastasis. MMP-9 is secreted as zymogen with prodomain, gelatin-binding domain consisting of three contiguous fibronectin type II units, catalytic domain, proline-rich linker region, and C-terminal hemopexin-like domain. It can degrade a variety of substrates, including gelatin, collagens type IV, V, XIV, a2-macroglobulin, elastin, vitronectin, and proteoglycans.

The sequence (Accession # NP_004985.2) corresponding to the catalytic domain (aa 112-445) of Human MMP-9 was expressed in E. coli. The recombinant human MMP-9 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-9 Catalytic Domain is ~40 kDa.

Specifications

Chemistry
UniProt number
  • P14780 (pro-MMP-9)
Molecular Mass/ Weight
  • 40 kDa
Modification
Conjugation
  • Unconjugated
Quantity & Purity
Concentration
  • lot dependent
Purification Method
  • Purified
Purity
  • >95%
Storage & stability
Form
  • In solution
Storage Buffer
  • 300 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl2, 20 µM ZnCl2, pH=7.5.
Storage Conditions
  • Store at -80 ºC. Avoid repeated freeze-thaw cycles.
Activity
Application
Biomarker Target
Specificity
  • Catalytic domain (aa 112-445) of Human MMP-9
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Host
Source / Species
  • human
Codes
Code Nacres
  • NA.27

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Citations

FoxO4 regulates TNF{alpha}-directed smooth muscle cell migration by activating matrix metalloproteinase 9 gene transcription.

Mol Cell Biol . 2007 Jan 22 ; 27(7) 2676 | DOI : 10.1128/MCB.01748-06.

  • H. Li
  • et al