Recombinant Anti-ADAM12 Antibody, Rabbit Monoclonal sinobiological 10896-R737

$171.00
In stock
SKU
10896-R737
Catalog No.SizePrice (USD)
10896-R737-5050 µL$177.58
10896-R737-100100 µL$340.51

General Information

Product nameRecombinant Anti-ADAM12 Antibody, Rabbit Monoclonal
Validated applicationsWB (FAQ Protocol)
Species reactivityReacts with: Human
SpecificityHuman ADAM12
ImmunogenRecombinant Human ADAM12 protein (Catalog#10896-H08H)
PreparationThis antibody was obtained from a rabbit immunized with purified, recombinant Human ADAM12 (rh ADAM12; Catalog#10896-H08H; NP_003465.3; Met1-Ser513).
SourceMonoclonal Rabbit IgG Clone #737
PurificationProtein A
Formulation0.2 μm filtered solution in PBS
ConjugateUnconjugated
FormLiquid
ShippingThis antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
StorageThis antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.

Synonyms: Anti-ADAM12-OT1 Antibody; Anti-CAR10 Antibody; Anti-MCMP Antibody; Anti-MCMPMltna Antibody; Anti-MLTN Antibody; Anti-MLTNA Antibody; Anti-UNQ346/PRO545 Antibody

Image / Experimental Information

Image 1 DescriptionAnti-ADAM12 rabbit monoclonal antibody at 1:500 dilution Lane A: A431 Whole Cell Lysate Lysates/proteins at 30 μg per lane. Secondary Goat Anti-Rabbit IgG H&L (Dylight800) at 1/10000 dilution. Developed using the Odyssey technique. Performed under reducing conditions. Predicted band size:100 kDa Observed band size:100 kDa
Image 1 Alt TextHuman ADAM12 Western blot (WB) 6622
Image 1 URLSource image

Background Information

Full NameADAM metallopeptidase domain 12
DescriptionThe 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.
Related Pathways
  • Notch Signaling
  • Actin Dynamics Signaling Pathway
  • MAPK-Erk Pathway
  • Autophagy Pathway
References
  1. 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.
  2. Kveiborg M, et al. (2008) Cellular roles of ADAM12 in health and disease. Int J Biochem Cell Biol. 40(9): 1685-702.
  3. Harsha A, et al. (2008) ADAM12: a potential target for the treatment of chronic wounds. J Mol Med. 86(8): 961-9.
  4. Jacobsen J, et al. (2009) Targeting ADAM12 in human disease: head, body or tail? Curr Pharm Des. 15(20): 2300-10.
  5. Baertling F, et al. (2010) ADAM12 is expressed by astrocytes during experimental demyelination. Brain Res. 1326: 1-14.

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