Recombinant human MMP13 protein (ab134452)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Active: Yes
- Suitable for: SDS-PAGE, Functional Studies
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Product name
Recombinant human MMP13 protein
See all MMP13 proteins and peptides -
Biological activity
The specific activity is >0.5 U/mg. 1 U is the activity that hydrolyzes 1 mmol peptide (7-methoxycoumarin-4-yl) acetyl-Pro-Leu-Gly-Leu-(3-[2, 4-dinitrophenyl]-L-2, 3-diamino-propionyl)-Ala-Arg-NH2 (Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg) within 1 min. -
Purity
> 90 % SDS-PAGE. -
Expression system
Escherichia coli -
Accession
-
Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM LPDDDVQGIQSLYGPGDEDPN -
Predicted molecular weight
19 kDa -
Amino acids
104 to 274
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Preparation and Storage
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Alternative names
- CLG 3
- CLG3
- Collagenase 3
see all -
Function
Degrades collagen type I. Does not act on gelatin or casein. Could have a role in tumoral process. -
Tissue specificity
Seems to be specific to breast carcinomas. -
Involvement in disease
Defects in MMP13 are the cause of spondyloepimetaphyseal dysplasia Missouri type (SEMD-MO) [MIM:602111]. 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) [MIM:602111]. 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. -
Sequence similarities
Belongs to the peptidase M10A family.
Contains 4 hemopexin-like domains. -
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. -
Cellular localization
Secreted > extracellular space > extracellular matrix. - Information by UniProt