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AB227435

Recombinant human MMP13 protein (Active)

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(1 Publication)

Recombinant human MMP13 protein (Active) is a Human Fragment protein, in the 104 to 274 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, FuncS.

View Alternative Names

Collagenase 3, Matrix metalloproteinase-13, MMP-13, MMP13

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Functional Studies - Recombinant human MMP13 protein (Active) (AB227435)
  • FuncS

Supplier Data

Functional Studies - Recombinant human MMP13 protein (Active) (AB227435)

The activity of ab227435 is ≥ 200 mU/mg based on its ability to hydrolyze a FRET-based MMP-13 substrate.

SDS-PAGE - Recombinant human MMP13 protein (Active) (AB227435)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human MMP13 protein (Active) (AB227435)

4-20% SDS-PAGE analysis of 5 μg ab227435.

Recombinant protein loaded under reducing conditions and stained with Coomassie Blue.

The protein shows a predicted MW of ~ 20.5 kDa.

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag C-Terminus

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

This enzyme has a specific activity of ≥200 mU/mg based on its ability to hydrolyze a FRET-based MMP-13 quenched substrate and results in increase of fluorescence, which can be detected at Ex/Em = 325/393 nm.

One unit is the amount of enzyme that will hydrolyze 1.0 μmole of MMP-13 substrate per minute at pH 7.5 and 37°C.

Accession

P45452

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 10.269% Trehalose, 0.727% Dibasic monohydrogen potassium phosphate, 0.248% Potassium phosphate monobasic

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

This product is manufactured by BioVision, an Abcam company and was previously called P1230 MMP-13, Catalytic Domain, Human Recombinant. P1230-10 is the same size as the 10 μg size of ab227435.
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Sequence info

[{"sequence":"YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPN","proteinLength":"Fragment","predictedMolecularWeight":"20.5 kDa","actualMolecularWeight":null,"aminoAcidEnd":274,"aminoAcidStart":104,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P45452","tags":[{"tag":"His","terminus":"C-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Matrix metallopeptidase 13 (MMP-13) also called collagenase 3 is an enzyme with an approximate molecular mass of 54 kDa. It plays a significant role in the breakdown of extracellular matrix components particularly collagen. MMP-13 is expressed in several tissues including cartilage skin and bone. Its expression sees an increase during tissue remodeling and in pathological conditions. MMP-13 also participates in processes like wound healing and embryonic development making it a focal point for understanding tissue dynamics.
Biological function summary

Matrix metallopeptidase 13 contributes extensively to the degradation of collagen type II a major component of cartilage. As a zinc-dependent endopeptidase MMP-13 is part of the MMP family which facilitates the remodeling of the extracellular matrix. MMP-13 is involved in the proteolytic cascade working in conjunction with other MMPs and elastase to mediate tissue repair and turnover. It does not form complexes but acts in concert with other enzymes to execute its physiological functions effectively.

Pathways

Matrix metallopeptidase 13 significance is most noted in the cartilage degradation pathway. It interacts with other MMPs such as MMP-1 and MMP-9 to efficiently break down extracellular matrix components. These interactions highlight its role in the regulation of matrix metalloproteinase activity within the connective tissue degradation pathway. These pathways are key during normal connective tissue remodeling and in pathological processes illustrating the essential roles of MMPs in maintaining tissue homeostasis.

Matrix metallopeptidase 13 has strong associations with osteoarthritis and rheumatoid arthritis. It contributes to cartilage destruction intensifying the progression of these disorders due to its potent collagenolytic activity. Other proteins like MMP-9 and MMP-14 are also involved in these processes potentially amplifying tissue damage in affected joints. Understanding how MMP-13 and related proteins drive these diseases offers potential therapeutic targets for slowing disease progression and enhancing joint health.
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Specifications

Form

Lyophilized

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General info

Function

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 CCN2. 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 CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.

Sequence similarities

Belongs to the peptidase M10A family.

Post-translational modifications

The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro).. N-glycosylated.. Tyrosine phosphorylated by PKDCC/VLK.

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Product protocols

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Target data

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 CCN2. 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 CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.
See full target information MMP13
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Nature cardiovascular research 1:67-84 PubMed35599984

2022

Aortic intimal resident macrophages are essential for maintenance of the non-thrombogenic intravascular state.

Applications

Unspecified application

Species

Unspecified reactive species

Gloria E Hernandez,Feiyang Ma,Guadalupe Martinez,Nadia B Firozabadi,Jocelynda Salvador,Lih Jiin Juang,Jerry Leung,Peng Zhao,Diego A López,Reza Ardehali,Anna E Beaudin,Christian J Kastrup,Matteo Pellegrini,Matthew J Flick,M Luisa Iruela-Arispe
View all publications
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