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A2351

Anti-ADAM-8, Propeptide Domain antibody produced in rabbit

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

Synonim(y):

Anti-A Disintegrin And Metalloproteinase-8, Anti-CD156, Anti-MS2

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Informacje o tej pozycji

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
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.

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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Ta pozycja
HPA064637AV53618HPA008879
conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

biological source

rabbit

biological source

rabbit

biological source

rabbit

biological source

rabbit

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

Gene Information

human ... ADAM8(101)
pig ... ADAM8(100156146)
rat ... Tubgcp2(309098)

Gene Information

human ... ADAM8(101)

Gene Information

human ... ADAM7(8756)

Gene Information

human ... ADAM7(8756)

UniProt accession no.

P78325

UniProt accession no.

P78325

UniProt accession no.

Q9H2U9

UniProt accession no.

Q9H2U9

technique(s)

western blot: 1:1,000

technique(s)

immunohistochemistry: 1:1000- 1:2500

technique(s)

western blot: suitable

technique(s)

immunohistochemistry: 1:200-1:500


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Klasa składowania

10 - Combustible liquids



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Powiązane treści


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
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
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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SKUNUMER GTIN
A2351-100UG04061837879500

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