ADAM8; CD156; MS2

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Product Preparation
A synthetic peptide corresponding to the human CD156b at Pro- domain. This sequence is identical among human, mouse and/or rat origins.
CD156b is a type I transmembrane glycoprotein belong to the ADAM (a disintegrin and metalloprotease domain) family. This single-pass type-1 824 aa transmembrane glycoprotein contains a signal sequence, an extracellular domain (pro-domain, catalytic domain, disintegrin-cysteine-rich domain, glycosylation sites), transmembrane and cytoplasmic domain. CD156b is a multi-domain protein that includes a Zn-dependent protease domain in the extracellular portion.  It releases the soluble forms of TNF and TGFa from cells.  CD156b is identified by its ability to cleave the transmembrane form of TNF between Ala-76 and Val-77 to generate the soluble form. CD156b is therefore a prospective therapeutic target in human cancer. CD156b is expressed on T cells, neutrophils, endothelial cells, monocytes, dendritic cells, macrophages, polymorphonuclear leukocytes and myocytes. And non-lymphoid tissues including heart, placenta, brain, muscle.  
The Rabbit IgG is purified by Epitope Affinity Purification
This antibody recognizes ~100 kDa of human CD156b. It also reacts with mouse. The other species are not tested.
This affinity purified antibody is supplied in sterile Phosphate buffered saline (pH7.2) containing antibody stabilizer.
The antibodies are stable for 12 months from date of receipt when stored at –20oC. The antibodies can be stored at 2oC-8oC for one month without detectable loss of activity. Avoid repeated freezing-thawing cycles.
Gene ID
Applications/Suggested Working Dilutions
Western Blot
0.1-1 µg/ml
0.01-0.1 µg/ml
2-5 µg/ml
2-10 µg/ml
Flow cytometry
5-10 µg/ml
Order Info
Catalog #: 601-270
Lot #: See the label
Size: 100 ug
Host: Rabbit
Isotyping: Rabbit IgG
Applications: IHC(P), WB
Reactivity: Hu, Ms, Rt
Price: $ 280.00
Gooz,P., et al. ADAM-17 regulates endothelial cell morphology, proliferation, and in vitro angiogenesis Biochem. Biophys. Res. Commun. 380 (1), 33-38 (2009).
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