MMP-8/Matrix Metalloproteinase-8 Recombinant Protein | MMP-8 recombinant protein

Recombinant Human MMP-8/Matrix Metalloproteinase-8 Protein (C-His)

Cat. Num. AAA2557187

• Gene Names: MMP8; HNC; CLG1; MMP-8; PMNL-CL
• Purity: >90% as determined by reducing SDS-PAGE.
• Synonyms: MMP-8/Matrix Metalloproteinase-8; Recombinant Human MMP-8/Matrix Metalloproteinase-8 Protein (C-His); Neutrophil collagenase; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL; MMP8; CLG1; MMP-8 recombinant protein

• Host: Human Cells
• Purity/Purification: >90% as determined by reducing SDS-PAGE.
• Form/Format: Lyophilized from a 0.2 mum filtered solution of PBS, pH7.4.
• Sequence: Phe21-Gly467
• Sequence Length: 467

• Species: Human
• Endotoxin: < 1.0 EU per mug as determined by the LAL method.
• Fusion Tag: C-His
• Preparation and Storage: Lyophilized protein should be stored at < -20 degree C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7 degree C for 2-7 days. Aliquots of reconstituted samples are stable at < -20 degree C for 3 months.

Related Product Information for MMP-8 recombinant protein

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

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-alpha and GM-CSF. MMP8 is capable of cleaving types I, II and III triple-helical collagen, gelatin peptides, fibronectin, proteoglycans, aggrecan, serpins, beta-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.

NCBI and Uniprot Product Information

• NCBI GI #: 4505221
• NCBI GeneID: 4317
• NCBI Accession #: NP_002415.1
• NCBI GenBank Nucleotide #: NP_002415.1
• UniProt Accession #: P22894
• Molecular Weight: Molecular Mass: 52.8kDa; Actual Protein Molecular Mass: 58kDa
• NCBI Official Full Name: neutrophil collagenase isoform 1 preproprotein
• NCBI Official Synonym Full Names: matrix metallopeptidase 8
• NCBI Official Symbol: MMP8
• NCBI Official Synonym Symbols: HNC; CLG1; MMP-8; PMNL-CL
• NCBI Protein Information: neutrophil collagenase
• UniProt Protein Name: Neutrophil collagenase
• UniProt Gene Name: MMP8
• UniProt Synonym Gene Names: CLG1; MMP-8; PMNL-CL
• UniProt Entry Name: MMP8_HUMAN

NCBI Description

This gene encodes a member of the matrix metalloproteinase (MMP) family of proteins. These proteins are involved in the breakdown of extracellular matrix in embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Proteolysis at different sites on this protein results in multiple active forms of the enzyme with distinct N-termini. This protein functions in the degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2015]

Uniprot Description

MMP8: Can degrade fibrillar type I, II, and III collagens. Belongs to the peptidase M10A family.

Protein type: Secreted; EC 3.4.24.34; Protease; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 11q22.3

Cellular Component: proteinaceous extracellular matrix; extracellular space; extracellular region

Molecular Function: zinc ion binding; metalloendopeptidase activity; serine-type endopeptidase activity; calcium ion binding

Biological Process: collagen catabolic process; extracellular matrix disassembly; extracellular matrix organization and biogenesis; proteolysis