Caldesmon 1 (CALD1) (pSer759) antibody

Details for Product No. ABIN649407
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Antigen
Synonyms CALD1, caldesmon, si:bz30i22.4, si:rp71-30i22.4, zgc:56389, CDM, H-CAD, HCAD, L-CAD, LCAD, NAG22, 4833423D12Rik, AI195384, AV071549, AW536160, C920027I18Rik, l-Cad
Epitope
pSer759
(22), (11), (7), (4), (3), (3), (3), (3), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Human
(148), (76), (71), (26), (25), (17), (6), (2), (2), (2), (1), (1), (1), (1)
Host
Rabbit
(120), (38)
Clonality
Monoclonal
Conjugate
Un-conjugated
(5), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1)
Application
Western Blotting (WB)
(120), (55), (46), (43), (36), (20), (18), (13), (8), (4), (4), (4), (4), (3), (1)
Pubmed 4 references available
Quantity 100 μL
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Catalog No. ABIN649407
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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.
Alternative Name Caldesmon
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).
Synonyms: CALD1, CAD, CDM, Caldesmon
Molecular Weight 70-80 kDA
Gene ID 800
UniProt Q05682
Research Area Phospho-specific antibodies, Protein Modifications, Cell Structure
Application Notes The suggested dilution is: WB: = 1:1500-3000
Comment

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).

Restrictions For Research Use only
Format Liquid
Buffer 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Caldesmon Antibody Phospho (pS759) can be stored at -20°C for up to 12 months from time of receipt.
Expiry Date 12 months
Background publications 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).

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