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Rat Anti-MMP9 (AA 20-730) Recombinant Antibody (CBFYM-2428) (CBMAB-M2615-FY)


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Summary

Host Animal
Rat
Specificity
Mouse
Clone
CBFYM-2428
Antibody Isotype
IgG2a
Application
ELISA(Det)

Basic Information

Immunogen
Mouse myeloma cell line NS0-derived recombinant mouse MMP-9, Ala20-Pro730
Specificity
Mouse
Antibody Isotype
IgG2a
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
Buffer
PBS
Concentration
LYOPH
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 20-730

Target

Full Name
Matrix Metallopeptidase 9
Introduction
Proteins of the matrix metalloproteinase 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
Entrez Gene ID
17395
UniProt ID
P41245
Alternative Names
Matrix Metallopeptidase 9; Matrix Metalloproteinase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase); EC 3.4.24.35; CLG4B; MMP-9; GELB; Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase); Matrix Metalloproteinase-9;
Function
Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:2551898, PubMed:1480034, PubMed:12879005).

Could play a role in bone osteoclastic resorption (By similarity).

Cleaves KiSS1 at a Gly-|-Leu bond (PubMed:12879005).

Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:32883094).

Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed:1480034).

Degrades fibronectin but not laminin or Pz-peptide.
Biological Process
Cellular response to cadmium ion Source: CAFA
Cellular response to reactive oxygen species Source: CAFA
Cellular response to UV-A Source: UniProtKB
Collagen catabolic process Source: GO_Central
Embryo implantation Source: Ensembl
Endodermal cell differentiation Source: UniProtKB
Ephrin receptor signaling pathway Source: Reactome
Extracellular matrix disassembly Source: Reactome
Extracellular matrix organization Source: GO_Central
Leukocyte migration Source: InterPro
Macrophage differentiation Source: UniProtKB
Negative regulation of apoptotic process Source: CACAO
Negative regulation of cation channel activity Source: UniProtKB
Negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: CACAO
Negative regulation of epithelial cell differentiation involved in kidney development Source: ARUK-UCL
Negative regulation of intrinsic apoptotic signaling pathway Source: CACAO
Ossification Source: InterPro
Positive regulation of apoptotic process Source: Ensembl
Positive regulation of cell migration Source: ARUK-UCL
Positive regulation of DNA binding Source: CACAO
Positive regulation of epidermal growth factor receptor signaling pathway Source: CACAO
Positive regulation of keratinocyte migration Source: BHF-UCL
Positive regulation of protein phosphorylation Source: CACAO
Positive regulation of receptor binding Source: UniProtKB
Positive regulation of release of cytochrome c from mitochondria Source: CACAO
Positive regulation of vascular associated smooth muscle cell proliferation Source: BHF-UCL
Proteolysis Source: UniProtKB
Regulation of neuroinflammatory response Source: ARUK-UCL
Response to amyloid-beta Source: ARUK-UCL
Skeletal system development Source: Ensembl
Cellular Location
Extracellular matrix
Involvement in disease
Intervertebral disc disease (IDD):
A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.
Metaphyseal anadysplasia 2 (MANDP2):
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.
PTM
Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.
N- and O-glycosylated.
More Infomation

Rashid, Z. A., & Bardaweel, S. K. (2023). Novel matrix metalloproteinase-9 (MMP-9) inhibitors in cancer treatment. International journal of molecular sciences, 24(15), 12133.

Al-Sadi, R., Engers, J., Haque, M., King, S., Al-Omari, D., & Ma, T. Y. (2021). Matrix Metalloproteinase-9 (MMP-9) induced disruption of intestinal epithelial tight junction barrier is mediated by NF-κB activation. PLoS One, 16(4), e0249544.

Wang, L., Deng, L., Yuan, R., Liu, J., Li, Y., & Liu, M. (2020). Association of matrix metalloproteinase 9 and cellular fibronectin and outcome in acute ischemic stroke: a systematic review and meta-analysis. Frontiers in Neurology, 11, 523506.

Walter, L., Canup, B., Pujada, A., Bui, T. A., Arbasi, B., Laroui, H., ... & Garg, P. (2020). Matrix metalloproteinase 9 (MMP9) limits reactive oxygen species (ROS) accumulation and DNA damage in colitis-associated cancer. Cell death & disease, 11(9), 767.

Barillari, G. (2020). The impact of matrix metalloproteinase-9 on the sequential steps of the metastatic process. International Journal of Molecular Sciences, 21(12), 4526.

Mondal, S., Adhikari, N., Banerjee, S., Amin, S. A., & Jha, T. (2020). Matrix metalloproteinase-9 (MMP-9) and its inhibitors in cancer: A minireview. European journal of medicinal chemistry, 194, 112260.

Li, T., Li, X., Feng, Y., Dong, G., Wang, Y., & Yang, J. (2020). The role of matrix metalloproteinase-9 in atherosclerotic plaque instability. Mediators of inflammation, 2020.

Silva, N. J., Nagashima, M., Li, J., Kakuk‐Atkins, L., Ashrafzadeh, M., Hyde, D. R., & Hitchcock, P. F. (2020). Inflammation and matrix metalloproteinase 9 (Mmp‐9) regulate photoreceptor regeneration in adult zebrafish. Glia, 68(7), 1445-1465.

Hariono, M., Nuwarda, R. F., Yusuf, M., Rollando, R., Jenie, R. I., Al-Najjar, B., ... & Wahab, H. A. (2019). Arylamide as potential selective inhibitor for matrix metalloproteinase 9 (MMP9): design, synthesis, biological evaluation, and molecular modeling. Journal of chemical information and modeling, 60(1), 349-359.

Xia, B., Hong, T., He, X., Hu, X., & Gao, Y. (2019). A circular RNA derived from MMP9 facilitates oral squamous cell carcinoma metastasis through regulation of MMP9 mRNA stability. Cell transplantation, 28(12), 1614-1623.

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

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