M6309
Anti-Matrix Metalloproteinase-23, Hinge Region antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
别名:
Anti-MMP-23
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关于此项目
UNSPSC Code:
12352203
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA (i), IHC (f), IP, WB
Citations:
2
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.
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.
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.
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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