Matrix Metalloproteinase-13 Recombinant Protein | MMP 13 recombinant protein

Recombinant Human Matrix Metalloproteinase-13

Cat. Num. AAA142458

• Gene Names: MMP13; CLG3; MANDP1; MMP-13
• Purity: Greater than 90% as determined by SDS-PAGE.
• Synonyms: Matrix Metalloproteinase-13; Recombinant Human Matrix Metalloproteinase-13; MMP 13 Human; Matrix Metalloproteinase-13 Human Recombinant; CLG3; MANDP1; Collagenase 3; Matrix metalloproteinase-13; MMP-13; MMP13; MMP 13 recombinant protein

• Host: E Coli
• Purity/Purification: Greater than 90% as determined by SDS-PAGE.
• Form/Format: The MMP-13 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.; Sterile Filtered clear solution.
• Sequence: MGSSHHHHHH SSGLVPRGSH MGSYNVFPRT LKWSKMNLTY RIVNYTPDMT HSEVEKAFKK AFKVWSDVTP LNFTRLHDGI ADIMISFGIK EHGDFYPFDG PSGLLAHAFP PGPNYGGDAH FDDDETWTSS SKGYNLFLVA AHEFGHSLGL DHSKDPGALM FPIYTYTGKS HFMLPDDDVQ GIQSLYGPGD EDPNPKHPKT PDKCDPSLSL DAITSLRGET MIFKDRFFWR LHPQQVDAEL FLTKSFWPEL PNRIDAAYEH PSHDLIFIFR GRKFWALNGY DILEGYPKKI SELGLPKEVK KISAAVHFED TGKTLLFSGN QVWRYDDTNH IMDKDYPRLI EEDFPGIGDK VDAVYEKNGY IYFFNGPIQF EYSIWSNRIV RVMPANSILW C
• Sequence Length: 471

Related Product Information for MMP 13 recombinant protein

Description: MMP-13 produced in E Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (104-471 a.a.) and having a molecular mass of 44.7 kDa. MMP-13 is fused to a 23 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.

Introduction: Latent recombinant human pro-collagenase (MMP-13) also called collagenase-3 truncated from C-terminal.Matrix Metalloproteinase-13 (MMP-13) is an enzyme that is a member of the MMP extracellular protease family. Extracellular protease enzymes, by virtue of their broad substrate specificities1, play a role in both normal and disease states of tissue proliferation. Among the targets of MMP-13 are collagen, gelatin, entactin, pro-TNF-a, and chemokine SDF-11-4.MMP-13 is found in its latent form as a 52-56 kDa glycosylated proenzyme. Upon cleavage the 22-46 kDa5 MMP-1 becomes active in extracellular matrix remodeling.Because of the prominent role that MMP-1 plays in cell migration and metastasis, it is an important target for inhibition screening.

Product Categories/Family for MMP 13 recombinant protein

Enzymes; Matrix Metalloproteinase

NCBI and Uniprot Product Information

• NCBI GI #: 4505209
• NCBI GeneID: 4322
• NCBI Accession #: NP_002418.1
• NCBI GenBank Nucleotide #: NM_002427.3
• UniProt Accession #: P45452; Q6NWN6; A8K846; B2RCZ3
• Molecular Weight: 53,820 Da
• NCBI Official Full Name: collagenase 3 preproprotein
• NCBI Official Synonym Full Names: matrix metallopeptidase 13
• NCBI Official Symbol: MMP13
• NCBI Official Synonym Symbols: CLG3; MANDP1; MMP-13
• NCBI Protein Information: collagenase 3; matrix metallopeptidase 13 (collagenase 3); matrix metalloproteinase 13 (collagenase 3)
• UniProt Protein Name: Collagenase 3
• UniProt Gene Name: MMP13
• UniProt Synonym Gene Names: MMP-13
• UniProt Entry Name: MMP13_HUMAN

NCBI Description

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. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]

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: Secreted, signal peptide; Secreted; EC 3.4.24.-; Protease

Chromosomal Location of Human Ortholog: 11q22.3

Cellular Component: extracellular space; proteinaceous extracellular matrix; extracellular region

Molecular Function: collagen binding; zinc ion binding; metalloendopeptidase activity; calcium ion binding

Biological Process: collagen catabolic process; extracellular matrix disassembly; extracellular matrix organization and biogenesis; cellular protein metabolic process; proteolysis; bone mineralization; endochondral ossification

Disease: Spondyloepimetaphyseal Dysplasia, Missouri Type