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  • 产品名称：ADAMMetallopeptidaseDomain12(ADAM12)(AA29-513)(Active)protein(Histag)

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  • 产品厂商：ACROBiosystems
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简单介绍：
ADAMMetallopeptidaseDomain12(ADAM12)(AA29-513)(Active)protein(Histag)
详情介绍：
Characteristics rh ADAM12 is fused with 6 xHis tag at the C terminus, and has a calculated MW of 55.2 kDa (Arg 29 - Asp 513, Propeptide 20.1 kDa + mature form 34.5 kDa). The rh ADAM12 (Arg 29 - Asp 513) was cleaved into the propeptide and the mature form. The reducing (R) protein migrates as 65 kDa, 46 kDa and 23 kDa in SDS-PAGE due to glycosylation, corresponding to the proprotein form, the mature form and the propeptide respectively.
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured by its ability to cleave IGFBP-3. The bioactivity was measured in 100μL reaction mixture containing 20 μg/mL of rhADAM12, 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, pH 7.5.

SDS-PAGE: due to glycosylation, corresponding to the proprotein form, the mature form and the propeptide respectively.
Background A Disintegrin And Metalloprotease 12 (ADAM12) is also known as Meltrin-alpha and MCMP, is a member of the ADAM and MDC (Metalloprotease, Disintegrin, Cysteine-rich) protein family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biological processes involving in diverse processes such as asthma, development, angiogenesis and cancer through their activities in cell adhesion/fusion, membrane protein shedding, and signal transduction. Over 30 members have been identified and about half of them are active metalloproteases such as ADAM8, 9, 10, 12 and 17/TACE. ADAM12 has four Isoform, Isoform 1 is expressed in placenta and skeletal, cardiac, and smooth muscle. Isoform 2 seems to be expressed only in placenta or in embryo and fetus. Both forms were expressed in some tumor cells lines. ADAM12 Involved in skeletal muscle regeneration, specifically at the onset of cell fusion and also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors.
Molecular Weight 55.2 kDa (Proprotein), 34.5 kDa (Mature Form) and 20.1 kDa (propeptide)
UniProt O43184
Research Area Proteolysis / Ubiquitin, Metalloprotease, Extracellular Matrix, Proteases
Pathways EGFR Signaling Pathway
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 100 mM NaCl, pH 7.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for ADAM Metallopeptidase Domain 12 (ADAM12) (AA 29-513) (Active) protein (His tag) (ABIN2180562) Human ADAM12, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained o...
Background publications Bourd-Boittin, Le Pabic, Bonnier, LHelgoualch, Théret: "RACK1, a new ADAM12 interacting protein. Contribution to liver fibrogenesis." in: The Journal of biological chemistry, Vol. 283, Issue 38, pp. 26000-9, 2008 (PubMed).

Bartholin, Destaing, Forissier, Martel, Maguer-Satta, Jurdic, Rimokh: "FLRG, a new ADAM12-associated protein, modulates osteoclast differentiation." in: Biology of the cell / under the auspices of the European Cell Biology Organization, Vol. 97, Issue 7, pp. 577-88, 2005 (PubMed).

Abram, Seals, Pass, Salinsky, Maurer, Roth, Courtneidge: "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells." in: The Journal of biological chemistry, Vol. 278, Issue 19, pp. 16844-51, 2003 (PubMed).

Iba, Albrechtsen, Gilpin, Fröhlich, Loechel, Zolkiewska, Ishiguro, Kojima, Liu, Langford, Sanderson, Brakebusch, Fässler, Wewer: "The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading." in: The Journal of cell biology, Vol. 149, Issue 5, pp. 1143-56, 2000 (PubMed).