Target：MMP-11

Gene Name：MMP11

Protein Name：Stromelysin-3

Human Gene Id：4320

Human Swiss Prot No：P24347

Mouse Gene Id：17385

Mouse Swiss Prot No：Q02853

Rat Gene Id：25481

Rat Swiss Prot No：Q499S5

Immunogen：The antiserum was produced against synthesized peptide derived from human MMP-11. AA range:61-110

Specificity：MMP-11 Polyclonal Antibody detects endogenous levels of MMP-11 protein.

Formulation：Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Source：Polyclonal, Rabbit,IgG

Dilution：WB 1:500 - 1:2000. IHC 1:100 - 1:300. IF 1:200 - 1:1000. ELISA: 1:20000. Not yet tested in other applications.

Purification：The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Concentration：1 mg/ml

Storage Stability：-15°C to -25°C/1 year(Do not lower than -25°C)

Other Name：MMP11;STMY3;Stromelysin-3;SL-3;ST3;Matrix metalloproteinase-11;MMP-11

Observed Band(KD)：60kD

Background： 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 MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, the enzyme encoded by this gene is activated intracellularly by furin within the constitutive secretory pathway. Also in contrast to other MMP's, this enzyme cleaves alpha 1-proteinase inhibitor but weakly degrades structural proteins of the extracellular matrix. [provided by RefSeq, Jul 2008],

Function：cofactor:Binds 1 calcium ion 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:May play an important role in the progression of epithelial malignancies.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Belongs to the peptidase M10A family.,similarity:Contains 4 hemopexin-like domains.,tissue specificity:Specifically expressed in stromal cells of breast carcinomas.,

Subcellular Location：Secreted, extracellular space, extracellular matrix .

Expression：Specifically expressed in stromal cells of breast carcinomas.