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Merck
CN

M5184

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

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
MFCD03097008
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA (i), IHC (f), IP, WB
Citations:
2

Key Documents

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biological source

rabbit

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

Quality Level

200

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.

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.
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).

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

Regulatory Information

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Certificates of Analysis (COA)

Lot/Batch Number
090K1488

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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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