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Merck
CN

M4677

Sigma-Aldrich

Anti-Matrix Metalloproteinase-2, Hinge Region antibody produced in rabbit

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

Synonym(s):

Anti-MMP-2

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About This Item

MDL number:
UNSPSC Code:
12352203
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biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

clone

polyclonal

form

buffered aqueous glycerol solution

mol wt

antigen 72 kDa

species reactivity

human

concentration

~1 mg/mL

technique(s)

western blot: 1:1,000 using a concentrated cell culture medium from a stimulated human cell line (M 2928)

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... MMP2(4313)

Immunogen

synthetic peptide corresponding to the hinge region of human matrix metalloproteinase-2 (gelatinase-A)

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biochem/physiol Actions

By immunoblotting the antibody reacts against the reduced and native protein. It reacts with free MMP-2 or MMP-2 bound to TIMP-2.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 50% glycerol and 15 mM sodium azide.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Shokoufeh Mahmoodzadeh et al.
Cardiovascular research, 85(4), 719-728 (2009-10-29)
Female sex and sex hormones contribute to cardiac remodelling. 17beta-estradiol (E2) is involved in the modulation of extracellular matrix composition and function. Here, we analysed the effect of E2 on matrix metalloproteinase (MMP)-2 gene expression and studied the underlying molecular
Sonia Métayer et al.
Biology of reproduction, 66(5), 1219-1229 (2002-04-23)
The testicular and epididymal fluids of ram, boar, and stallion were analyzed by means of one-dimensional and two-dimensional gelatin gel zymography. Five main gelatinolytic bands were revealed in the ram and at least seven were observed in the boar and
Norbert Berndt et al.
Nature protocols, 6(11), 1775-1791 (2011-11-01)
The importance of the post-translational lipid modifications farnesylation and geranylgeranylation in protein localization and function coupled with the critical role of prenylated proteins in malignant transformation has prompted interest in their biology and the development of farnesyl transferase and geranylgeranyl

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