Reactive species
Human;Mouse;Rat;Monkey
Applications
WB;IHC;IF;ELISA
Antibody type
Polyclonal Antibody
Immunogen
The antiserum was produced against synthesized peptide derived from human MMP-7. AA range:218-267
Specificity
MMP-7 Polyclonal Antibody detects endogenous levels of MMP-7 protein.
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
WB: 1/500 - 1/2000. IHC: 1/100 - 1/300. ELISA: 1/40000.. IF 1:50-200
Purification process
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Other name
MMP7; MPSL1; PUMP1; Matrilysin; Matrin; Matrix metalloproteinase-7; MMP-7; Pump-1 protease; Uterine metalloproteinase
Background
matrix metallopeptidase 7(MMP7) Homo sapiens This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Proteins in this 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. The encoded preproprotein is proteolytically processed to generate the mature protease. This secreted protease breaks down proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal hemopexin domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes on chromosome 11. This gene exhibits elevated expression levels in multiple human cancers. [provided by RefSeq, Jan 2016],
Function
catalytic activity:Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).,cofactor:Binds 2 calcium ions per subunit.,cofactor:Binds 2 zinc ions per subunit.,domain: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.,function:Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.,similarity:Belongs to the peptidase M10A family.,
