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For research use only.

Verified Samples Verified Samples in WB: HT29
Verified Samples in IHC: Human liver cancer
Verified Samples in IF: Rat lung
Dilution WB 1:500-1:2000,  IHC 1:100-1:300,  IF 1:200-1:1000
Isotype IgG
Host Rabbit
Reactivity Human,  Mouse,  Rat,  Monkey
Applications WB,  IHC-p,  IF
Clonality Polyclonal
Immunogen Synthesized peptide derived from the C-terminal region of human MMP-2
Abbre MMP-2
Synonyms 72 kDa gelatinase,  72kD type IV collagenase,  CLG 4,  CLG 4A,  CLG4,  CLG4A,  Collagenase Type 4 alpha,  Collagenase type IV A,  Gelatinase A,  Gelatinase alpha,  Gelatinase neutrophil,  Matrix ,  Matrix metallopeptidase 2 gelatinase A 72kDa gelatinase 72kDa type IV collagenase
Swissprot
Calculated MW 74 kDa
Observed MW 74 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. Membrane. Nucleus. Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes.
Concentration 1 mg/mL
Buffer Phosphate buffered solution, pH 7.4, containing 0.05% stabilizer, 0.5% protein protectant and 50% glycerol.
Purification Method 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 Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro.PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.
Other Clones

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Unconjugated

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