Human MMP8 peptide

Specificity

Neutrophils.

Nature

Synthetic

Tag/Conjugate

Unconjugated

SequenceSimilarities

Belongs to the peptidase M10A family.Contains 4 hemopexin-like domains.

Alternative Names

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Purity

70 - 90% by HPLC.

Format

Liquid

Preservative

None

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.

Entrez Gene ID

Antigen Description

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is stored in secondary granules within neutrophils and is activated by autolytic cleavage. Its function is degradation of type I, II and III collagens. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]

Function

calcium ion binding; metalloendopeptidase activity; serine-type endopeptidase activity; zinc ion binding;

Synonyms

MMP8; matrix metallopeptidase 8 (neutrophil collagenase); HNC; CLG1; MMP-8; PMNL-CL; neutrophil collagenase; PMNL collagenase; matrix metalloproteinase-8; matrix metalloproteinase 8 (neutrophil collagenase);