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Mouse MMP-9 (20-471) Protein, His Tag (Pro-form, MALS verified)

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MM9-M52H1-50ug
$360.00
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MM9-M52H1-1mg
$2,225.00
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MM9-M52H1
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Product Details
Performance Data
Reviews & Citations
Resources
  • Product Details
  • Performance Data
  • Reviews & Citations
  • Important Statement
  • Resources
Synonyms

MMP9, CLG4B, GELB, MANDP2, Gelatinase B

Source

Mouse MMP-9 (20-471), His Tag (MM9-M52H1) is expressed from human 293 cells (HEK293). It contains AA Ala 20 - Pro 471 (Accession # P41245-1). It needs to be activated by agents such as APMA in vitro to have hydrolytic activity.

Predicted N-terminus: Ala 20

Molecular Characterization
Other Tags and Version Biotin & Other Labeled Version

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 52.0 kDa. The protein migrates as 60-66 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>95% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

Formulation

Supplied as 0.2 μm filtered solution in 25 mM Tris, 150 mM NaCl, pH7.5, Glycerol with trehalose as protectant.

Contact us for customized product form or formulation.

Shipping and Storage

This product is supplied and shipped on dry ice.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • The product MUST be stored at -20°C or lower upon receipt;
  • -20°C for 3 months under sterile conditions.
ACRO Quality Management System

Background

Matrix metallopeptidase 9 (MMP-9) is also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), CLG4B, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. Structurally, MMP9 maybe be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.