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100μL $ 380.00
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For research use only.

Verified Samples Verified Samples in WB: MCF7
Dilution WB 1:500-1:1000,  
Isotype IgG
Host Rabbit
Reactivity Human
Applications WB
Clonality Rabbit Monoclonal
Immunogen Recombinant Human MMP-2 protein
Abbre MMP2
Synonyms TBE,  CLG,  Matrix Metalloproteinase,  MMP,  CLG4,  CLG4A,  MMP-2,  MMP-II,  MONA,  TBE-1,  MMP2,  72 kDa Gelatinase,  72 kDa Type IV Collagenase,  Gelatinase A,  Matrix Metalloproteinase-2,  72kD type IV collagenase,  72kDa gelatinase,  72kDa type IV collagenase),  CLG 4,  CLG 4A,  Collagenase Type 4 alpha,  Collagenase type IV A,  Gelatinase alpha,  Gelatinase neutrophil,  Matrix metallopeptidase 2 gelatinase A 72kDa gelatinase 72kDa type IV collagenase,  Matrix Metalloproteinase 2,  Matrix metalloproteinase 2 (gelatinase A,  Matrix metalloproteinase II,  MMP 2,  MMP II,  Neutrophil gelatinase,  PEX,  TBE 1
Swissprot
Calculated MW 73 kDa
Observed MW 73 kDa

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.

Cellular Localization Secreted, Extracellular space, Extracellular matrix, Nucleus, Cytoplasm, Mitochondrion.
Tissue Specificity Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.
Concentration 1 mg/mL
Buffer 0.2 μm filtered solution in PBS
Purification Method Protein A
Research Areas Cardiovascular,  Cancer,  Cell Biology,  Metabolism
Clone No. 12F8
Conjugation Unconjugated
Storage This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.
Shipping Ice bag
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 a 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.
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