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AB227435

Recombinant human MMP13 protein (Active)

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.

別名を表示する

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

2 Images
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

精製度

>95% SDS-PAGE

発現系

Escherichia coli

タグ

His tag C-Terminus

アプリケーション

SDS-PAGE, FuncS

applications

生物活性

Yes

生物学的活性

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.

アクセッション番号

P45452

アニマルフリー

No

キャリアフリー

No

Human

再構成

Reconstitute the lyophilized protein in 30% glycerol to a final concentration 1.0 mg/ml and incubate the reconstituted protein at 25 °C for 15 minutes.

バッファー組成

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

storage-buffer

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>" } } }

製品の詳細

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.

配列情報

[{"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"}]}]

出荷温度及び保存条件

出荷温度
Blue Ice
短期保存温度
-20°C
長期保存温度
-20°C
保管に関する情報
Avoid freeze / thaw cycle
True

補足情報

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.

製品の性状

製品の状態

Lyophilized

一般的な情報

機能

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.

配列の類似性

Belongs to the peptidase M10A family.

翻訳後修飾

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.

製品プロトコール

ターゲットの情報

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

文献 (1)

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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
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