MMP 9 Protein (AA 20-707)

Catalog No. ABIN2666513

This Recombinant MMP 9 protein is expressed in HEK-293 Cells.

Quick Overview for MMP 9 Protein (AA 20-707) (ABIN2666513)

Target: MMP 9 (MMP9) (Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase) (MMP9))

Protein Type: Recombinant

Biological Activity: Active

Origin: Human

Source: HEK-293 Cells

Application: Biochemical Assay (BCA)

Purity: > 95 % , as determined by Coomassie stained SDS-PAGE.

Product Details

Protein Characteristics: AA 20-707

Sterility: 0.22 μm filtered

Endotoxin Level:

Less than 1.0 EU per μg of protein as determine by the LAL method.

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

Biological activity: Human MMP-9 cleaves the peptide substrate Mca-PLGL-Dpa-AR-NH2 with an activity above 1000 pmol/min/μg.

Restrictions: For Research Use only

Handling

Format: Liquid

Reconstitution: For maximum results, quick spin vial prior to opening.

Buffer: 0.22 μm filtered protein solution is in TCN (25 mM TRIS, 10 mM CaCl2, 150 mM NaCl, pH 7.5).

Handling Advice: Avoid repeated freeze/thaw cycles.

Storage: -20 °C

Storage Comment: Unopened vial can be stored at -70°C for six months.

Target Details

Target: MMP 9 (MMP9) (Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase) (MMP9))

Alternative Name: MMP-9

Background: MMP-9 is a member of the matrix metalloproteinase family of proteins (MMPs). Members of this family are structurally related, zinc-containing enzymes that degrade the extracellular matrix (ECM) and connective tissue proteins. Proteolytic activities of MMPs play an important role in vascular remodeling, cellular migration, and processing of ECM proteins and adhesion molecules. MMP-9 consists of a prodomain, catalytic domain, hinge region, and hemopexin domain, and is secreted as an inactive zymogen that becomes activated extracellularly. Among all secreted MMPs, only MMP-9 has been found to form a homodimer. The native dimeric form of MMP-9 was found to be present in neutrophils. It is the hemopexin domain of MMP-9 that mediates the homodimerization of the molecule and the heterodimerization with CD44. The most relevant natural activators of proMMP-9 are unknown. MMP-9 activation may be mediated by removal of the prodomain by serine proteases, other MMPs, or it may be a direct response to oxidative stress that disrupts the cysteine switch. MMP-9 is capable of processing cytokines and chemokines. For example, it is reported to release the biologically active form of vascular endothelial growth factor (VEGF), indicating that MMP-9 may play a crucial role in the formation of new blood vessels. MMP-9 participates in the migration of immune cells as demonstrated by MMP-9 knockout mice after antigen challenge. Increased MMP-9 expression and activity has been observed to be related to various cancers, as it may contribute to the release of metastatic cells from the bulk tumor as well as their entrance at the site of metastasis by degrading proteins in the ECM and basement membrane.

Molecular Weight: This 722 amino acid recombinant protein has a predicted molecular mass of approximately 80 kDa. The protein migrates at about 92 kDa in DTT-reducing conditions and 250 kDa in non-reducing conditions by SDS-PAGE.The predicted N-terminal amino acid is Ala.

Pathways: Cellular Response to Molecule of Bacterial Origin, Positive Regulation of Immune Effector Process, CXCR4-mediated Signaling Events