MMP-2 Polyclonal Antibody (D-AB-10399L)
For research use only.
| Verified Samples |
Verified Samples in WB: RAW264.7, NIH/3T3, Mouse uterus, Rat liver |
| Dilution | WB 1:500-1:1000 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Mouse, Rat |
| Applications | WB |
| Clonality | Polyclonal |
| Immunogen | Recombinant Human MMP-2 Protein expressed by E.coli |
| Abbre | MMP-2 |
| Synonyms | 72 kDa Gelatinase, 72 kDa Type IV Collagenase, CLG4, CLG4A, Gelatinase A, MMP-2, MMP-II, MMP2, MONA, Matrix Metalloproteinase-2, TBE-1 |
| Swissprot | |
| Calculated MW | 74 kDa |
| Observed MW |
69 kDa-72 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Antigen Affinity Purification |
| Research Areas | Cancer, Cell Biology, Cardiovascular, Metabolism |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack,upon receipt,store it immediately at the temperature recommended. |
| background | Matrix Metalloproteinase-2 (MMP-2) is an enzyme that degrades components of the extracellular matrix and thus plays a pivotal role in cell migration during physiological and pathological processes. MMP-2 expression is dependent on extracellular matrix metalloproteinase inducer (EMMPRIN),Her2/neu,growth factors,cytokines,and hormones. Pro-MMP-2 activation needs MT1-MMP and TIMP-2 contribution. MMP-2 is changed in distribution and increased in amount in the ventral cochlear nucleus after unilateral cochlear ablation. A low level of MMP-2 is linked to favorable prognosis in patients with a hormone receptor-negative tumor,usually associated with high risk. As a zymogen requiring proteolytic activation for catalytic activity,MMP-2 has been implicated broadly in the invasion and metastasis of many cancer model systems,including human breast cancer (HBC). Blocking MMP-2 secretion and activation during breast carcinoma development may decrease metastasis. The detection of active MMP-2 alone or the rate of pro-MMP-2 and active MMP-2 is considered a very sensitive indicator of cancer metastasis. Modulation of MMP-2 expression and activation through specific inhibitors and activators may thus provide a new mechanism for breast cancer treatment. |
Other Clones
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Unconjugated
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