|+1 404 474 4654|
|+1 888 205 9894 (TF)|
Caldesmon 1 (CALD1) (pSer759) antibody
|Synonyms||CDM, H-CAD, L-CAD, NAG22, MGC21352, AI195384, AV071549, AW536160, MGC30319, 4833423D12Rik, C920027I18Rik, CALD1, caldesmon, zgc:56389, si:bz30i22.4, si:rp71-30i22.4, DKFZp459K021|
Alternatives Western Blotting (WB)
|4 references available|
|Price||507.14 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 2 to 3 Business Days|
|Description||Other names: CALD1, CAD, CDM, Caldesmon|
|Characteristics||Rabbit Monoclonal Antibody|
|Specificity||A phospho-specific peptide corresponding to residues surrounding Serine 759 of human Caldesmon was used as an immunogen. The antibody only detects Caldesmon phosphorylated at Serine 759.|
|Molecular Weight||70-80 kDA|
Background: Caldesmon is a smooth muscle and nonmuscle regulatory protein that interacts with actin, myosin, tropomyosin, and calmodulin (1,2). Smooth muscle caldesmon is an elongated molecule with a calmodulin, tropomyosin, and actin-binding region at the C-terminus and a myosin-binding domain at the N-terminus (3). Caldesmon stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, caldesmon inhibits the actomyosin ATPase by binding to F-actin. This inhibition is reduced by calcium-calmodulin and is promoted by tropomyosin (4). Phosphorylation of caldesmon by extracellular signal-regulated kinase (ERK) and p38 mitogen-activated protein (MAP) kinases in smooth muscle are important for actin and tropomyosin binding, and actomyosin inhibitory activity. In intact vascular smooth muscle Caldesmon is phosphorylated by proline-directed protein kinases, members of the MAP kinase family, suggesting that caldesmon phosphorylation by MAP kinase may modulate smooth muscle contraction (5).
|Application Notes||The suggested dilution is: WB: ~~ 1:1500~3000|
|Buffer||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Caldesmon Antibody Phospho (pS759) can be stored at -20°C for up to 12 months from time of receipt.|
|Research Area||Phospho-specific antibodies, Protein Modifications, Cell Structure|
|Restrictions||For Research Use only|
Humphrey, Herrera-Sosa, Gonzalez et al.: "Cloning of cDNAs encoding human caldesmons." in: Gene, Vol. 112, Issue 2, pp. 197-204, 1992 (PubMed).
Bryan: "Caldesmon: fragments, sequence, and domain mapping." in: Annals of the New York Academy of Sciences, Vol. 599, pp. 100-10, 1990 (PubMed).
Bryan, Imai, Lee et al.: "Cloning and expression of a smooth muscle caldesmon." in: The Journal of biological chemistry, Vol. 264, Issue 23, pp. 13873-9, 1989 (PubMed).
Fraser, Copeland, Bing et al.: "The inhibitory complex of smooth muscle caldesmon with actin and tropomyosin involves three interacting segments of the C-terminal domain 4." in: Biochemistry, Vol. 36, Issue 18, pp. 5483-92, 1997 (PubMed).