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AB51072

Anti-MMP13 antibody [EP1263Y]

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(86 Publications)

Rabbit Recombinant Monoclonal MMP13 antibody. Suitable for WB and reacts with Human samples. Cited in 86 publications.

View Alternative Names

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

1 Images
Western blot - Anti-MMP13 antibody [EP1263Y] (AB51072)
  • WB

Lab

Western blot - Anti-MMP13 antibody [EP1263Y] (AB51072)

All lanes:

Western blot - Anti-MMP13 antibody [EP1263Y] (ab51072) at 1/1000 dilution

All lanes:

HeLa (Human cervix adenocarcinoma epithelial cell) whole cell lysates at 15 µg

Secondary

All lanes:

Western blot - Goat Anti-Rabbit IgG H&L (HRP) (<a href='/en-us/products/secondary-antibodies/goat-rabbit-igg-h-l-hrp-ab97051'>ab97051</a>) at 1/20000 dilution

Predicted band size: 54 kDa

Observed band size: 60 kDa

false

  • Carrier free

    Anti-MMP13 antibody [EP1263Y] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EP1263Y

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

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Reactivity data

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Product details

Species reactivity
Mouse, Rat: We have preliminary internal testing data to indicate this antibody may not react with these species.
Please contact us for more information.

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.2 - 7.4 Preservative: 0.01% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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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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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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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 (86)

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

Frontiers in immunology 16:1633334 PubMed40821826

2025

A novel carboxamide bromodomain inhibitor attenuates osteoarthritis via epigenetic repression of NF-κB and MAPK signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Hyemi Lee,Seong Jae Han,Subin Ok,Kwang Min Lee,Seungseok Choi,Injoo Yoon,Somang Choi,Jina Kim,Serim Ryu,Min-Hee Son,In-Hyun Lee,Chanmi Cho,Siyoung Yang

Nature communications 16:1094 PubMed39904978

2025

Regulation of senescence-associated secretory phenotypes in osteoarthritis by cytosolic UDP-GlcNAc retention and O-GlcNAcylation.

Applications

Unspecified application

Species

Unspecified reactive species

Donghyun Kang,Jeeyeon Lee,Geunho Yook,Sehan Jeong,Jungkwon Shin,Mi-Sung Kim,Yi-Jun Kim,Hyeryeon Jung,Jinsung Ahn,Tae Woo Kim,Moon Jong Chang,Chong Bum Chang,Seung-Baik Kang,Won Ho Yang,Yong-Ho Lee,Jin Won Cho,Eugene C Yi,Chanhee Kang,Jin-Hong Kim

The Journal of biological chemistry 301:108247 PubMed39894218

2025

A BRAF-activated noncoding RNA attenuates clear cell renal cell carcinoma via repression of glucose-6-phosphate dehydrogenase.

Applications

Unspecified application

Species

Unspecified reactive species

Wenjing Liu,Yueli Ni,Honggang Bai,Xiangjie Liu,Asif Shahzad,Kun Cui,Qiuxin Duan,Ziyuan Bai,Yurong Dong,Zihan Yi,Buqing Sai,Yingmin Kuang,Chen Guo,Yuechun Zhu,Qiao Zhang,Zhe Yang

Molecular medicine (Cambridge, Mass.) 30:253 PubMed39707183

2024

CXCL4 deficiency limits M4 macrophage infiltration and attenuates hyperoxia-induced lung injury.

Applications

Unspecified application

Species

Unspecified reactive species

Bingrui Yu,Siyuan Jia,Yu Chen,Rong Guan,Shuyu Chen,Wanwen Tang,Tianping Bao,Zhaofang Tian

Journal of orthopaedic surgery and research 19:826 PubMed39639339

2024

WTAP mediates IL-1β-induced chondrocyte injury by enhancing CA12 mRNA stability depending on m6A modification.

Applications

Unspecified application

Species

Unspecified reactive species

Gang Deng,Yizhou Xu,Zhengnan Li,Guangxuan Zeng

Bioactive materials 43:305-318 PubMed39399840

2024

An intra articular injectable Mitocelle recovers dysfunctional mitochondria in cellular organelle disorders.

Applications

Unspecified application

Species

Unspecified reactive species

Min Ju Lim,Hyeryeon Oh,Jimin Jeon,Chanmi Cho,Jin Sil Lee,Yiseul Hwang,Seok Jung Kim,Jung-Soon Mo,Panmo Son,Ho Chul Kang,Won Il Choi,Siyoung Yang

Antioxidants (Basel, Switzerland) 13: PubMed39199188

2024

Fucoxanthin Suppresses NF-κB, JNK, and p38-Associated MMP Expression in Arthritis Pathogenesis via Antioxidant Activity.

Applications

Unspecified application

Species

Unspecified reactive species

Hyemi Lee,Hahyeong Jang,Dahyoon Heo,Jae-In Eom,Cheol-Ho Han,Se-Min Kim,Yoo-Seob Shin,Cheol-Ho Pan,Siyoung Yang

Nature communications 15:1024 PubMed38310093

2024

5-aminosalicylic acid suppresses osteoarthritis through the OSCAR-PPARγ axis.

Applications

Unspecified application

Species

Unspecified reactive species

Jihee Kim,Gina Ryu,Jeongmin Seo,Miyeon Go,Gyungmin Kim,Sol Yi,Suwon Kim,Hana Lee,June-Yong Lee,Han Sung Kim,Min-Chan Park,Dong Hae Shin,Hyunbo Shim,Wankyu Kim,Soo Young Lee

International journal of molecular sciences 24: PubMed38139287

2023

WGA-M001, a Mixture of Total Extracts of and , Synergistically Alleviates Cartilage Destruction by Inhibiting ERK and NF-κB Signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Eunjeong Oh,Hahyeong Jang,Subin Ok,Jiwon Eom,Hyunyong Lee,Sung Hun Kim,Jong Hwa Kim,Yu Mi Jeong,Kyeong Jin Kim,Seung Pil Yun,Hyung-Jun Kwon,In-Chul Lee,Ji-Young Park,Siyoung Yang

Arthritis research & therapy 25:236 PubMed38057865

2023

Prokineticin 2 is a catabolic regulator of osteoarthritic cartilage destruction in mouse.

Applications

Unspecified application

Species

Unspecified reactive species

Jiye Yang,Youngnim Shin,Hwee-Jin Kim,Hyo-Eun Kim,Jang-Soo Chun
View all publications
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