Product Name :
Cleaved-MMP-23 (Y79) Peptide Applications :
Blocking Background :
Matrix metalloproteinases (MMPs) are highly homologous Zn2+ endopeptidases involved in extracellular matrix breakdown. MMP mediated extracellular remodeling occurs in normal physiological processes, such as embryonic development, reproduction and tissue remodeling, and disease processes, including arthritis and metastasis. MMP-23 exhibits sequence similarity with most MMPs, but displays a difference in domain structure. The MMP-23 protein contains prepro-, catalytic, cysteine-rich, Interleukin-1 receptor-related and proline-rich domains. Lacking a recognizable signal sequence, MMP-23 has a short prodomain. In addition, MMP-23 contains a single cysteine residue that can be part of the cysteine-switch mechanism operation for maintaining enzyme latency. MMP-23 is a membrane-anchored glycoprotein with type II topology. Subcellular localization is predominantly perinuclear. Alternative Name :
Matrix metalloproteinase-23; MMP 23; Femalysin; MIFR-1; Matrix metalloproteinase-21; MMP-21; Matrix metalloproteinase-22; MMP-22; Matrix metalloproteinase-23, soluble form; MMP23A; MMP21; MMP23B; MMP21; MMP22; MMP23 Swiss-Prot :
O75900 Product :
1 mg/ml in DI water. Purification&Purity :
Synthetic peptide Cleaved-MMP-23 (Y79). (Note: the amino acid sequence is proprietary). The purity is > 98%. Storage&Stability :
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles. Specificity :
This peptide can be used with studies using BS7054 Cleaved-MMP-23 (Y79) pAb.
Cleaved-MMP-23 (Y79) Peptide Applications :
Blocking Background :
Matrix metalloproteinases (MMPs) are highly homologous Zn2+ endopeptidases involved in extracellular matrix breakdown. MMP mediated extracellular remodeling occurs in normal physiological processes, such as embryonic development, reproduction and tissue remodeling, and disease processes, including arthritis and metastasis. MMP-23 exhibits sequence similarity with most MMPs, but displays a difference in domain structure. The MMP-23 protein contains prepro-, catalytic, cysteine-rich, Interleukin-1 receptor-related and proline-rich domains. Lacking a recognizable signal sequence, MMP-23 has a short prodomain. In addition, MMP-23 contains a single cysteine residue that can be part of the cysteine-switch mechanism operation for maintaining enzyme latency. MMP-23 is a membrane-anchored glycoprotein with type II topology. Subcellular localization is predominantly perinuclear. Alternative Name :
Matrix metalloproteinase-23; MMP 23; Femalysin; MIFR-1; Matrix metalloproteinase-21; MMP-21; Matrix metalloproteinase-22; MMP-22; Matrix metalloproteinase-23, soluble form; MMP23A; MMP21; MMP23B; MMP21; MMP22; MMP23 Swiss-Prot :
O75900 Product :
1 mg/ml in DI water. Purification&Purity :
Synthetic peptide Cleaved-MMP-23 (Y79). (Note: the amino acid sequence is proprietary). The purity is > 98%. Storage&Stability :
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles. Specificity :
This peptide can be used with studies using BS7054 Cleaved-MMP-23 (Y79) pAb.
Blocking peptide available as BS7054PP