Recombinant Human MMP8/CLG1 Protein (His Tag) | PKSH033578

Recombinant Human MMP8/CLG1 Protein (His Tag) | PKSH033578 | Gentaur US, UK & Europe Disrtribition

Synonyms: Neutrophil collagenase; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL;MMP8; CLG1

Active Protein: N/A

Activity: Recombinant Human MMP-8 is produced by our Mammalian expression systemand the target gene encoding Phe21-Gly467 is expressed with a 10His tag at the C-terminus.

Protein Construction: Recombinant Human MMP-8 is produced by our Mammalian expression systemand the target gene encoding Phe21-Gly467 is expressed with a 10His tag at the C-terminus.

Fusion Tag: C-His

Species: Human

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 52.8 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of PBS, pH7.4.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP8 (neutrophil collagenase) is expressed in neutrophils, where it is stored in specific granules. MMP8 release from the neutrophils is stimulated by various factors such as interleukins 1 and 8, TNF-α and GM-CSF. MMP8 is capable of cleaving types I, II and III triple-helical collagen, gelatin peptides, fibronectin, proteoglycans, aggrecan, serpins, β-casein and peptides such as angiotensin and substance P. In addition to its function in phagocytosis, MMP8 has a high capacity for infiltrating connective tissue, and is implicated in the breakdown of the extracellular matrix in diseases such as rheumatoid arthritis. Structurally, MMP8 consists of several domains: a pro-domain that is cleaved upon activation, a catalytic domain containing the zinc-binding site, a short hinge region and a hemopexin-like domain. MMP8 is heavily glycosylated.

Research Area: Signal Transduction, Cell biology, Cardiovascular, Cancer,