Data & Images
|Product Name||Anti-MMP-12 Antibody|
|Description||Rabbit IgG polyclonal antibody for Macrophage metalloelastase(MMP12) detection. Tested with WB in Human.|
|Cite This Product||Anti-MMP-12 Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA2146)|
|Replacement Item||This antibody may replace the following items: sc-101449|sc-102424|sc-102426|sc-12361|sc-133151|sc-19993|sc-30072|sc-31805|sc-31807|sc-31809|sc-46656|sc-52455|sc-65990|sc-7632|sc-80544|sc-9149 from Santa Cruz Biotechnology.|
*Our Boster Guarantee covers the use of this product in the above tested applications.
**For positive and negative control design, consult "Tissue specificity" under Protein Target Info.
|Recommended Detection Systems||Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
*Blocking peptide can be purchased at $50. Contact us for more information
**Boster also offers various secondary antibodies for Immunoflourescecne and IHC. Take advantage of the buy 1 primary antibody get 1 secondary antibody for free promotion for the entire year 2018!
|Immunogen||A synthetic peptide corresponding to a sequence at the C-terminus of human MMP12(428-444aa KIDAVFYSKNKYYYFFQ).|
|Cross Reactivity||No cross reactivity with other proteins|
|Contents||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.|
|Concentration||Add 0.2ml of distilled water will yield a concentration of 500ug/ml.|
|Storage||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Purification||Immunogen affinity purified.|
Protein Target Info (Source: Uniprot.org)
You can check the tissue specificity below for information on selecting positive and negative control.
|Protein Name||Macrophage metalloelastase|
|Molecular Weight||54002 MW|
|Protein Function||May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.|
|Tissue Specificity||Found in alveolar macrophages but not in peripheral blood monocytes.|
|Sequence Similarities||Belongs to the peptidase M10A family.|
|Subcellular Localization||Secreted, extracellular space, extracellular matrix .|
|Alternative Names||Macrophage metalloelastase;MME;184.108.40.206;Macrophage elastase;ME;hME;Matrix metalloproteinase-12;MMP-12;MMP12;HME;|
|Research Areas|||cardiovascular|angiogenesis|adhesion / ecm|matrix metalloproteinases|mmp| signal transduction|cytoskeleton / ecm|extracellular matrix|ecm enzymes| cancer|invasion/microenvironment|mmps|tumor biomarkers| cardiovascular|atherosclerosis|thrombosis||
Background for Macrophage metalloelastase
Dilution Ratios/Recommended Concentrations
At Boster we strive to provide the best Anti-MMP-12 Antibody by testing all applications on non-spiked tissues and cell lines to ensure that the affinity of the antibody is enough to react to the endogenouse level of the target protein. Read more about our QC panel here.
|Recommended dilution ratios are listed below:|
Western blot, 0.1-0.5μg/ml, Human|
**Boster provides high sensitivity secondary antibody kits for Western blotting and IHC. For more info see Related Products below.
Anti-MMP-12 Antibody Images
Click the images to enlarge.
Lane 1: SMMC Cell Lysate
Lane 2: HEPA Cell Lysate
Lane 3: HELA Cell Lysate
Lane 4: K562 Cell Lysate
Lane 5: MCF-7 Cell Lysate
1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,