MMP12 Antibody (YA7031)
(Synonyms: Mme, Mmel, Mmp12, Macrophage metalloelastase, MME, Matrix metalloproteinase-12, MMP-12)Based on 1 Customer Validation
MMP12 Antibody (YA7031) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to MMP12.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, IHC-F, IF-Tissue
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Reactivity :
Human
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Formulation:
Supplied in 10mM TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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IHC-F
IHC-F: Immunohistochemistry-Frozen
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IF-Tissue
IF-Tissue: Immunofluorescence-Tissue
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|---|---|---|---|---|
| Dilution Ratio | 1:500-2000 | 1:100-500 | 1:100-500 | 1:100-500 |
Product Details
MMP12 Antibody (YA7031) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to MMP12.
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Host Rabbit
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Clonality Recombinant
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 42-48 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 42 kDa
A synthesized peptide derived from human MMP12: 405-470.
Endogenous
affinity purified by Protein A
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 10mM TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
MMP-12, also known as macrophage metalloelastase, is a zinc-dependent extracellular matrix protease predominantly produced by activated macrophages and is characterized by potent elastolytic activity involved in tissue injury and remodeling processes[1][2]. Mechanistically, MMP-12 participates in extracellular matrix degradation, macrophage migration, inflammatory signaling, and tissue remodeling, thereby linking innate immune responses to structural alterations in affected tissues[2][3]. In disease settings, elevated MMP-12 activity has been associated with chronic pulmonary disorders, including chronic obstructive pulmonary disease and emphysema, where elastin degradation contributes directly to pathological lung remodeling[2][4]. Experimental studies further demonstrate that MMP-12 regulates macrophage infiltration, inflammatory cytokine expression, vascular dysfunction, and pathological angiogenesis in ischemic retinopathy models, supporting its broader role in inflammatory and remodeling-associated diseases[3]. Compared with several related matrix metalloproteinases that display broader substrate repertoires, MMP-12 is distinguished by its strong elastase activity and prominent expression in inflammatory macrophages, making it particularly relevant to elastin-rich tissue remodeling and macrophage-driven pathology[1][2]. For experimental applications, genetic deletion or pharmacological inhibition of MMP-12 reduces inflammatory responses, macrophage recruitment, and pathological tissue remodeling in multiple disease models, supporting its utility as a mechanistic target for studying inflammation, extracellular matrix turnover, and disease progression[3][4].
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Subcellular Localization
Secreted, extracellular space, extracellular matrix
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Expression
Tissue_Specificity: Found in alveolar macrophages but not in peripheral blood monocytes
Induction: By exposure to bacterial lipopolysaccharides (LPS). Inhibited by dexamethasone -
Isoforms & Post-Translational Modification
P39900: 470 amino acids, molecular weight 54002 Da.
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SwissProt ID
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Synonyms
Mme, Mmel, Mmp12, Macrophage metalloelastase, MME, Matrix metalloproteinase-12, MMP-12
Documentation
References
[1]. Garbacki N, et al. Matrix metalloproteinase 12 silencing: a therapeutic approach to treat pathological lung tissue remodeling? Pulm Pharmacol Ther. 2009 Aug;22(4):267-78. [Content Brief]
[2]. Uniprotkb.
[3]. Li J, et al. Macrophage metalloelastase (MMP-12) deficiency mitigates retinal inflammation and pathological angiogenesis in ischemic retinopathy. PLoS One. 2012;7(12):e52699. [Content Brief]
[4]. Bhaskaran R, et al. Solution structure of inhibitor-free human metalloelastase (MMP-12) indicates an internal conformational adjustment. J Mol Biol. 2007 Dec 14;374(5):1333-44. [Content Brief]