MMP16 antibody (ab5709)

Product Name 

MMP16 antibody

Product type 

Primary antibodies

Description 

Rabbit polyclonal to MMP16

Immunogen 

Synthetic peptide, corresponding to amino acids 167-181 of Human MMP 16.

Reacts with 

Hu

Predicted to react 
(species key)

Ms, Rat
(Due to sequence homology)

Specificity 

This antibody specifically recognises MMP16, and does not cross-react with MMP1, 2, 3, 7, 8, 9 or 10.

Tested applications 
(see key)

ELISA, IP, WB

Abreviews 

Customer reviews (see key)

Read about Abreviews

Application notes 
(see key)

Recommended dilutions
ELISA: Use at a concentration of 0.1 - 1.0 µg/ml.
IP: Use 3-5µg for 10⁶ cells.
WB: Use at a concentration of 0.5 - 2.0 µg/ml. Detects a band of approximately 65 kDa.

Not tested in other applications.
Optimal dilutions/concentrations should be determined by the end user.

Positive control 
(see definition)

PMA stimulated A431 whole cell lysate.

Cellular localization 

Secreted protein; extracellular space; extracellular matrix

Research areas 

Cell Biology >> Proteolysis / Ubiquitin >> Proteolytic enzymes >> Metalloprotease >> MMPs
Cancer >> Invasion/microenvironment >> ECM >> Extracellular matrix >> MMPs
Cancer >> Invasion/microenvironment >> Angiogenesis >> ECM enzymes >> MMPs
Cardiovascular >> Angiogenesis >> Adhesion / ECM >> Matrix Metalloproteinases >> MMP

Relevance 

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zinc endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.
MMP16 induces the activation of pro gelatinase A (MMP2). It was identified as a membrane bound Metalloproteinase in normal and tumor cell lines. MMP16 is similar to the other MtMMPs; it contains a furin cleavage site, is membrane bound, and contains a cytoplasmic tail (MT4MMP lacks the tail, and may not be intercalated into the membrane). MMP16 is also known to be "shed" from the membrane in a soluble form. MT1MMP is known to function in activating a number of MMPs, chiefly MMP2, but that role has not been well described for the other MTMMPs. MMP16 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines.

Database links 

Raised in 

Rabbit

Clonality 

Polyclonal

Isotype 

IgG

Purity 

Immunogen affinity purified

Storage buffer 

Preservative: 0.02% Proclin
Constituents: PBS, pH 7.4

Form 

Liquid

Concentration 

0.500 mg/ml

Storage instructions 

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

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