Recombinant Human MMP13 protein is a Human Fragment protein, in the 104 to 471 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M G S Y N V F P R T L K W S K M N L T Y R I V N Y T P D M T H S E V E K A F K K A F K V W S D V T P L N F T R L H D G I A D I M I S F G I K E H G D F Y P F D G P S G L L A H A F P P G P N Y G G D A H F D D D E T W T S S S K G Y N L F L V A A H E F G H S L G L D H S K D P G A L M F P I Y T Y T G K S H F M L P D D D V Q G I Q S L Y G P G D E D P N P K H P K T P D K C D P S L S L D A I T S L R G E T M I F K D R F F W R L H P Q Q V D A E L F L T K S F W P E L P N R I D A A Y E H P S H D L I F I F R G R K F W A L N G Y D I L E G Y P K K I S E L G L P K E V K K I S A A V H F E D T G K T L L F S G N Q V W R Y D D T N H I M D K D Y P R L I E E D F P G I G D K V D A V Y E K N G Y I Y F F N G P I Q F E Y S I W S N R I V R V M P A N S I L W C
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
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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.
Collagenase 3, Matrix metalloproteinase-13, MMP-13, MMP13
Recombinant Human MMP13 protein is a Human Fragment protein, in the 104 to 471 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris-HCl buffer, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab177626 was purified by using conventional chromatography techniques.
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.
Belongs to the peptidase M10A family.
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).
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.
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.
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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15% SDS-PAGE analysis of ab177626 (3 μg).
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