Rabbit anti-Mouse Matrix Metalloproteinase 13 (MMP13) Polyclonal Antibody | anti-MMP13 antibody
Polyclonal Antibody to Matrix Metalloproteinase 13 (MMP13)
MGHHHHHHSGS- DPALS LDAITSLRGE TMIFKDRFFW RLHPQQVEAE LFLTKSFWPE LPNHVDAAYE HPSRDLMFIF RGRKFWALNG YDILEGYPRK ISDLGFPKEV KRLSAAVHFE NTGKTLFFSE NHVWSYDDVN QTMDKDYPRL IEEEFPGIGN KVDAVYEKNG YIYFFNGPIQ FEYSIWSNRI VR
Immunocytochemistry in formalin fixed cells: 1:100-500
Immunohistochemistry in formalin fixed frozen section: 1:100-500
Immunohistochemistry in paraffin section: 1:50-200
Enzyme-linked Immunosorbent Assay: 1:100-200
NCBI and Uniprot Product Information
NCBI Description
This gene encodes a member of the matrix metalloproteinase family that plays a role in wound healing, skeletal development and bone remodeling. The encoded protein is activated by the removal of an N-terminal activation peptide to generate a zinc-dependent endopeptidase enzyme that can cleave various native collagens, including types I - IV, X and XIV. Mice lacking the encoded protein display profound defects in growth plate cartilage as well as a delay in the endochondral bone development. Lack of the encoded protein also impairs the wound healing process due to reduced keratinocyte migration and vascular density at the wound site. This gene is located in a cluster of other matrix metalloproteinase genes on chromosome 9. [provided by RefSeq, Jun 2015]
Uniprot Description
MMP13: Degrades collagen type I. Does not act on gelatin or casein. Could have a role in tumoral process. Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia Missouri type (SEMD-MO). A bone disease characterized by moderate to severe metaphyseal changes, mild epiphyseal involvement, rhizomelic shortening of the lower limbs with bowing of the femora and/or tibiae, coxa vara, genu varum and pear-shaped vertebrae in childhood. Epimetaphyseal changes improve with age. Defects in MMP13 are the cause of metaphyseal anadysplasia type 1 (MANDP1). Metaphyseal anadysplasia consists of an abnormal bone development characterized by severe skeletal changes that, in contrast with the progressive course of most other skeletal dysplasias, resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia. Belongs to the peptidase M10A family.
Protein type: EC 3.4.24.-; Protease; Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 9|9 A1
Cellular Component: extracellular matrix; extracellular region; extracellular space; Golgi apparatus; intercellular canaliculus; lysosome; proteinaceous extracellular matrix
Molecular Function: calcium ion binding; calcium-dependent protein binding; collagen binding; fibronectin binding; hydrolase activity; low-density lipoprotein receptor binding; metal ion binding; metalloendopeptidase activity; metallopeptidase activity; peptidase activity; zinc ion binding
Biological Process: bone mineralization; cartilage development; cellular protein metabolic process; collagen catabolic process; endochondral ossification; extracellular matrix disassembly; heart development; peptide catabolic process; proteolysis