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Mouse Anti-MMP13 (AA 20-471) Recombinant Antibody (CBFYM-2356) (CBMAB-M2542-FY)

This product is mouse antibody that recognizes MMP13. The antibody CBFYM-2356 can be used for immunoassay techniques such as: ICC, IHC, IP, WB.
See all MMP13 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-2356
Antibody Isotype
IgG1
Application
ICC, IHC, IP, WB

Basic Information

Immunogen
Recombinant protein
Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Lyophilized
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 20-471

Target

Full Name
matrix metallopeptidase 13 (collagenase 3)
Introduction
This gene encodes a member of the peptidase M10 family of matrix metalloproteinases. Proteins in this family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. The encoded preproprotein is proteolytically processed to generate the mature protease. This protease cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. Mutations in this gene are associated with metaphyseal anadysplasia. This gene is part of a cluster of MMP genes on chromosome 11.
Entrez Gene ID
4322
UniProt ID
P45452
Alternative Names
Matrix Metallopeptidase 13; Matrix Metalloproteinase 13 (Collagenase 3); Collagenase 3; MMP-13; Matrix Metalloproteinase-13; EC 3.4.24.35; EC 3.4.24.22; EC 3.4.24.24
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.
Biological Process
Bone mineralization Source: Ensembl
Bone morphogenesis Source: UniProtKB
Cellular protein metabolic process Source: Ensembl
Collagen catabolic process Source: UniProtKB
Endochondral ossification Source: Ensembl
Extracellular matrix disassembly Source: UniProtKB
Extracellular matrix organization Source: GO_Central
Growth plate cartilage development Source: Ensembl
Proteolysis Source: ProtInc
Response to amyloid-beta Source: ARUK-UCL
Cellular Location
Extracellular matrix
Secreted
Involvement in disease
Spondyloepimetaphyseal dysplasia, Missouri type (SEMDM):
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.
Metaphyseal anadysplasia 1 (MANDP1):
A bone development disorder characterized by skeletal anomalies that 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.
Metaphyseal dysplasia, Spahr type (MDST):
An autosomal recessive, rare disease characterized by moderate short stature, mild genua vara, and radiographic signs of metaphyseal dysplasia, but no biochemical signs of rickets.
PTM
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.

Li, S., Pritchard, D. M., & Yu, L. G. (2022). Regulation and function of matrix metalloproteinase-13 in cancer progression and metastasis. Cancers, 14(13), 3263.

Luchian, I., Goriuc, A., Sandu, D., & Covasa, M. (2022). The role of matrix metalloproteinases (MMP-8, MMP-9, MMP-13) in periodontal and peri-implant pathological processes. International Journal of Molecular Sciences, 23(3), 1806.

Bendele, A. M., Neelagiri, M., Neelagiri, V., & Sucholeiki, I. (2021). Development of a selective matrix metalloproteinase 13 (MMP-13) inhibitor for the treatment of Osteoarthritis. European Journal of Medicinal Chemistry, 224, 113666.

Alwan, I. T., & Ghali, K. H. (2021). Association Risk of Metalomatrix Proteinase Enzymes Levels (MMP-1, MMP-9 And MMP-13) with Development of Rheumatoid Arthritis. Annals of the Romanian Society for Cell Biology, 11369-11378.

Oliveros Anerillas, L., Kingham, P. J., Lammi, M. J., Wiberg, M., & Kelk, P. (2021). Three-dimensional osteogenic differentiation of bone marrow mesenchymal stem cells promotes matrix metallopeptidase 13 (MMP13) expression in Type I collagen hydrogels. International Journal of Molecular Sciences, 22(24), 13594.

Hu, Q., & Ecker, M. (2021). Overview of MMP-13 as a Promising Target for the Treatment of Osteoarthritis. International journal of molecular sciences, 22(4), 1742.

Guimaraes-Stabili, M. R., de Medeiros, M. C., Rossi, D., Camilli, A. C., Zanelli, C. F., Valentini, S. R., ... & Rossa, C. (2021). Silencing matrix metalloproteinase-13 (Mmp-13) reduces inflammatory bone resorption associated with LPS-induced periodontal disease in vivo. Clinical Oral Investigations, 25, 3161-3172.

Wang, H., Li, H., Yan, Q., Gao, S., Gao, J., Wang, Z., & Sun, Y. (2021). Serum matrix metalloproteinase-13 as a diagnostic biomarker for cutaneous squamous cell carcinoma. BMC cancer, 21, 1-8.

Satish Kumar, K., Velayutham, R., & Roy, K. K. (2020). A systematic computational analysis of human matrix metalloproteinase 13 (MMP-13) crystal structures and structure-based identification of prospective drug candidates as MMP-13 inhibitors repurposable for osteoarthritis. Journal of Biomolecular Structure and Dynamics, 38(10), 3074-3086.

Zakaria, N. M., Mohamed, D. A., Omar, A. R., & Seif, A. M. (2019). Matrix Metalloproteinase-13 (MMP-13): A proposed Tumor Marker in Breast Carcinoma. Journal of Scientific Research in Science, 36(1), 358-366.

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For research use only. Not intended for any clinical use.

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