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M6309

Sigma-Aldrich

Anti-Matrix Metalloproteinase-23, Hinge Region antibody produced in rabbit

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

Synonym(s):

Anti-MMP-23

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About This Item

MDL number:
UNSPSC Code:
12352203

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous glycerol solution

mol wt

antigen (active form) 45 kDa
antigen (pro-form) 58 kDa

species reactivity

human

concentration

~1 mg/mL

technique(s)

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

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MMP14(4323)

General description

Matrix metalloproteinase-23B (MMP-23B) possesses regions which are rich in amino acids like proline and cysteine. The MMP-23B gene is localized on human chromosome 1p36.

Specificity

Reacts with reduced and non-reduced MMP-23. Recognizes the pro-form and active forms of MMP-23 as well as a series of further cleaved active forms.

Immunogen

synthetic peptide corresponding to the hinge region of human matrix metalloproteinase-23 (MIFR-2, CA-MMP).

Biochem/physiol Actions

Matrix metalloproteinase-23B (MMP-23B) is part of the matrix metalloproteinase family of proteins, which take part in the remodeling of the extracellular matrix.

Physical form

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

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Marzena Gajecka et al.
European journal of human genetics : EJHG, 13(2), 139-149 (2004-10-16)
Structural chromosome abnormalities have aided in gene identification for over three decades. Delineation of the deletion sizes and rearrangements allows for phenotype/genotype correlations and ultimately assists in gene identification. In this report, we have delineated the precise rearrangements in four
Matrix metalloproteinases.
H Nagase et al.
The Journal of biological chemistry, 274(31), 21491-21494 (1999-07-27)

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