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M5184

Sigma-Aldrich

Anti-Matrix Metalloproteinase-18, N-Terminal antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution

Synonym(s):

Anti-Xenopus collagenase, Anti-MMP-18, Anti-MMP-21-A, Anti-XMMP

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

species reactivity

Xenopus

concentration

~1 mg/mL

technique(s)

immunohistochemistry (frozen sections): suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot: 1:1,000

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

Xenopus laevis ... MMP19(108708572)

General description

Matrix metalloproteinase-18 (MMP-18) is an interstitial collagenase which possesses a special insertion domain of 37 amino acids. It is made up of around 626 amino acids. During metamorphosis, MMP-18 is controlled in tissue-dependent way.

Specificity

Reacts with reduced and non-reduced MMP-18. Recognizes the pro-form and the active forms of MMP-18. By immunoblotting, the antibody reacts with bands at 53 kDa and 51 kDa (proform).

Immunogen

synthetic peptide corresponding to the N-terminal of Xenopus matrix metalloproteinase-18 (Xenopus collagenase, collagenase-4)

Biochem/physiol Actions

Matrix metalloproteinase-18 (MMP-18) plays an important role in the development of Xenopus laevis.

Physical form

Solution in phosphate buffered saline, pH 7.4, containing 50% glycerol and 15 mM sodium azide

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Storage Class

10 - Combustible liquids


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M A Stolow et al.
Molecular biology of the cell, 7(10), 1471-1483 (1996-10-01)
Matrix metalloproteinases (MMPs) participate in extracellular matrix remodeling and degradation and have been implicated in playing important roles during organ development and pathological processes. Although it has been hypothesized for > 30 years that collagenase activities are responsible for collagen
M Yang et al.
The Journal of biological chemistry, 272(21), 13527-13533 (1997-05-23)
To study the role of matrix metalloproteinases (MMPs) in early vertebrate development, we cloned cDNAs for six different MMPs from the frog Xenopus laevis embryos at different stages of development and describe here a novel MMP called XMMP. Xenopus XMMP

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