A2351
Anti-ADAM-8, Propeptide Domain antibody produced in rabbit
~1 mg/mL, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-A Disintegrin And Metalloproteinase-8, Anti-CD156, Anti-MS2
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About This Item
Conjugate:
unconjugated
Clone:
polyclonal
Application:
WB
Citations:
4
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous glycerol solution
species reactivity
rat, human, pig
concentration
~1 mg/mL
technique(s)
western blot: 1:1,000
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... ADAM8(101)
pig ... ADAM8(100156146)
rat ... Tubgcp2(309098)
General description
ADAM8, a transmembrane glycoprotein, also known as MS2 and CD156, is a member of the metalloproteinase family containing disintegrin-like domains (ADAMs). ADAM8 is up-regulated in the central nervous system following neurogeneration and activation of glia, astrocytes, and microglia, suggesting that it may have a role in neuron-glia interactions. ADAM8 stimulates osteoclasts, suggesting a role in cell adhesion and cell fusion.
Anti-ADAM-8, propeptide domain antibody localizes human, porcine, and rat ADAM8 and does not react with other ADAMs. In immunoblotting assays against the reduced protein, the antibody recognizes 52kDa and 70kDa bands in conditioned media or cell lysates. In culture media, the 52kDa form is predominant.
Anti-ADAM-8, propeptide domain antibody localizes human, porcine, and rat ADAM8 and does not react with other ADAMs. In immunoblotting assays against the reduced protein, the antibody recognizes 52kDa and 70kDa bands in conditioned media or cell lysates. In culture media, the 52kDa form is predominant.
Immunogen
synthetic peptide corresponding to the propeptide domain of human ADAM-8.
Application
Anti-ADAM-8, propeptide domain antibody can be used for western blotting assays at a dilution of 1:1,000.
Physical form
Solution in 0.01 M phosphate buffered saline containing 50% glycerol and 0.05% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class
10 - Combustible liquids
Regulatory Information
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Uwe Schlomann et al.
The Journal of biological chemistry, 277(50), 48210-48219 (2002-10-10)
ADAMs (a disintegrin and metalloprotease domains) are metalloprotease and disintegrin domain-containing transmembrane glycoproteins with proteolytic, cell adhesion, cell fusion, and cell signaling properties. ADAM8 was originally cloned from monocytic cells, and its distinct expression pattern indicates possible roles in both
U Schlomann et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 20(21), 7964-7971 (2000-10-26)
ADAM proteases, defined by extracellular disintegrin and metalloprotease domains, are involved in protein processing and cell-cell interactions. Using wobbler (WR) mutant mice, we investigated the role of ADAMs in neurodegeneration and reactive glia activation in the CNS. We found that
S Yoshida et al.
International immunology, 2(6), 585-591 (1990-01-01)
cDNA clones which strongly hybridized with a 3.1 kb mRNA from mouse macrophages and macrophage cell lines and weakly with mRNA from P815 but not from a variety of other cell lines and tissues were isolated from cDNA libraries constructed
S J Choi et al.
Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, 16(5), 814-822 (2001-05-09)
We used polymerase chain reaction (PCR)-selective complementary DNA (cDNA) subtraction hybridization with an immortalized murine osteoclast (OCL) precursor cell line to identify genes that are highly expressed in OCLs compared with OCL precursors and which may be involved in the
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