protein

Recombinant Mouse Collagenase 3 (Mmp13)

MBS960550

0.5 mg (E-Coli)

1135 USD

Recombinant Protein

Recombinant Mouse Collagenase 3 (Mmp13)

Collagenase 3 (Mmp13)

Collagenase 3; EC=3.4.24.-; Matrix metalloproteinase-13; MMP-13

collagenase 3 preproprotein; Collagenase 3; collagenase 3; Collagenase-3; collagenase-1; interstitial collagenase; matrix metalloproteinase 13; matrix metalloproteinase-13; matrix metallopeptidase 13; Matrix metalloproteinase-13; MMP-13

Mmp13

Mmp13; Mmp13; Clg; Mmp1; MMP-13; MMP-13

MMP13_MOUSE

E Coli or Yeast or Baculovirus or Mammalian Cell

105-472

368

YNVFPR TLKWSQTNLT YRIVNYTPDM SHSEVEKAFR KAFKVWSDVT PLNFTRIYDG TADIMISFGT KEHGDFYPFD GPSGLLAHAF PPGPNYGGDA HFDDDETWTS SSKGYNLFIV AAHELGHSLG LDHSKDPGAL MFPIYTYTGK SHFMLPDDDV QGIQFLYGPG DEDPNPKHPK TPEKCDPALS LDAITSLRGE TMIFKDRFFW RLHPQQVEAE LFLTKSFWPE LPNHVDAAYE HPSRDLMFIF RGRKFWALNG YDILEGYPRK ISDLGFPKEV KRLSAAVHFE NTGKTLFFSE NHVWSYDDVN QTMDKDYPRL IEEEFPGIGN KVDAVYEKNG YIYFFNGPIQ FEYSIWSNRI VRVMPTNSIL WC

>90%

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

Species: Mus musculus (Mouse)

Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CTGF. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CTGF. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.

6678896

NP_032633.1

NM_008607.2

P33435

45kD

Activation Of Matrix Metalloproteinases Pathway (1001029); Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway (1001018); Collagen Degradation Pathway (1001030); Collagen Formation Pathway (1001016); Degradation Of The Extracellular Matrix Pathway (1001028); Endochondral Ossification Pathway (198336); Extracellular Matrix Organization Pathway (1001015); Matrix Metalloproteinases Pathway (198370)

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]

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.-; Secreted; Protease; Secreted, signal peptide. Cellular Component: Golgi apparatus; extracellular matrix; proteinaceous extracellular matrix; intercellular canaliculus; extracellular space; fibrillar collagen; lysosome; extracellular region. Molecular Function: peptidase activity; collagen binding; low-density lipoprotein receptor binding; hydrolase activity; metallopeptidase activity; zinc ion binding; fibronectin binding; metal ion binding; metalloendopeptidase activity; calcium ion binding; calcium-dependent protein binding. Biological Process: extracellular matrix disassembly; collagen catabolic process; cellular protein metabolic process; peptide catabolic process; cartilage development; receptor internalization; proteolysis; bone mineralization; endochondral ossification

0.5 mg (E-Coli)

1135 USD

0.05 mg (Baculovirus)

1135

0.5 mg (Yeast)

1365

0.05 mg (Mammalian-Cell)

1365

1 mg (E-Coli)

1805