Anti-ADAM12 Magnetic Beads Immunoprecipitation (IP) Kit

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抗ADAM12 磁気ビーズ免疫沈降(IP)キットの成分

Components Storage
Anti-ADAM12 Magnetic Beads1,3 2-8℃ for 12 months
NP40 Cell Lysis Buffer2 -20℃ for 12 months
5×TBST(pH7.4)  
1×TBST(pH7.4)  
ddH2O  
Alkaline Elution Buffer 2-8℃ for 12 months
Acidity Elution Buffer 2-8℃ for 12 months
Neutralization Buffer 2-8℃ for 12 months

【1】The IP KIT contains anti-ADAM12 magnetic Beads (2 mg/mL) in phosphate buffered saline (PBS, pH 7.4) with sodium azide (0.1%).

【2】Using NP-40 cell lysate buffer in the kit is required,otherwise,the magnetic beads may be precipitated.

【3】Shipping: Magnetic Beads kits are shipped at ambient temperature in which magnetic beads are provided in liquid buffer.

抗ADAM12 磁気ビーズ免疫沈降(IP)キットの製品説明

The Anti-ADAM12 magnetic Beads, conjugated with Anti-ADAM12 antibody, are used for immuneprecipitation (IP) of ADAM12 proteins which expressed in vitro expression systems. For IP, the beads are added to a sample containing ADAM12 proteins to form a bead-protein complex. The complex is removed from the solution manually using a magnetic separator. The bound ADAM12 proteins are dissociated from the magnetic beads using an elution buffer.

抗ADAM12 磁気ビーズ免疫沈降(IP)キット抗体の情報

抗体
Anti-ADAM12 Antibody(10896-R737)
免疫原
Recombinant Human ADAM12 protein (Catalog#10896-H08H)
交差反応
Human ADAM12
ソース
Monoclonal Human Rabbit IgG
調製
This antibody was obtained from a rabbit immunized with purified, recombinant Human ADAM12 (rh ADAM12; Catalog#10896-H08H; NP_003465.3; Met1-Ser513).
アプリケーション
Immunoprecipitation (IP), Minimum Protein Purification

Anti-ADAM12 Magnetic Beads Immunoprecipitation (IP) Kit: 別名

Anti-ADAM12-OT1ALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit; Anti-CAR10ALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit; Anti-MCMPALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit; Anti-MCMPMltnaALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit; Anti-MLTNALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit; Anti-MLTNAALCAM Magnetic Beads-Immunoprecipitatiopn (IP) Kit

ADAM12 背景情報

The ADAMs (a disintegrin and metalloprotease) comprise a family of multidomain proteins with metalloprotease, cell adhesion, and signaling activities. Human ADAM12, which is implicated in diseases such as cancer, is expressed in two splice forms, the transmembrane ADAM12-L and the shorter and soluble ADAM12-S. ADAM12, also known as and Meltrin alpha, is a member of the ADAM protein family, which contains one disintegrin domain, one EGF-like domain and one peptidase M12B domain. ADAM12 is synthesized as a zymogen with the prodomain keeping the metalloprotease inactive through a cysteine-switch mechanism. Maturation and activation of the protease involves the cleavage of the prodomain in the trans-Golgi or possibly at the cell surface by a furin-peptidase. It is a membrane-anchored metalloprotease, which has been implicated in activation-inactivation of growth factors that play an important role in wound healing, including heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) and IGF binding proteins. ADAM12 may also regulate cell-cell and cell-extracellular matrix contacts through interactions with cell surface receptors - integrins and syndecans - potentially influencing the actin cytoskeleton. Moreover, ADAM12 interacts with several cytoplasmic signaling and adaptor molecules through its intracellular domain, thereby directly transmitting signals to or from the cell interior. These ADAM12-mediated cellular effects appear to be critical events in both biological and pathological processes. In addition to protease activity, ADAM12 possesses cell binding and cell signaling properties. In many studies, ADAM12 overexpression has been correlated with disease, and ADAM12 has been shown to promote tumor growth and progression in cancer. On the other hand, protective effects of ADAM12 in disease have also been reported.
完全な名称
ADAM metallopeptidase domain 12
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    Autophagy Pathway
参考文献
  • Wewer UM, et al. (2006) ADAM12 is a four-leafed clover: the excised prodomain remains bound to the mature enzyme. J Biol Chem. 281(14): 9418-22.
  • Kveiborg M, et al. (2008) Cellular roles of ADAM12 in health and disease. Int J Biochem Cell Biol. 40(9): 1685-702.
  • Harsha A, et al. (2008) ADAM12: a potential target for the treatment of chronic wounds. J Mol Med. 86(8): 961-9.
  • Jacobsen J, et al. (2009) Targeting ADAM12 in human disease: head, body or tail? Curr Pharm Des. 15(20): 2300-10.
  • Baertling F, et al. (2010) ADAM12 is expressed by astrocytes during experimental demyelination. Brain Res. 1326: 1-14.
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