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CALD1 Antibody (Center)Purified Rabbit Polyclonal Antibody (Pab)
| Country | United States
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| Catalog # | Size | Availability | Price | |
| AP6609c | 0.1 mg 400 ul | In Stock | $ 255.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
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CALD1 Antibody (Center) - Product info | |
| Application | WB, IHC, FC
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| Primary Accession | Q05682 |
| Reactivity | Human |
| Concentration | 0.25 mg/ml |
| Isotype | Rabbit Ig |
| Calculated MW | 93231 Da |
CALD1 Antibody (Center) - Additional info | |
| Gene ID 800 | |
| Other Names CALD1; CAD; CDM; Caldesmon | |
| Target/Specificity This CALD1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 435~465 amino acids from the Center region of human CALD1. | |
| Dilution WB~~1:50~100WB~~1:1000 IHC~~1:10~50 FC~~1:10~50 | |
| Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. | |
| Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. | |
| Precautions CALD1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. | |
CALD1 Antibody (Center) - Protein Information | |
| Name CALD1 | |
| Synonyms CAD, CDM | |
| Function Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping Involved in Schwann cell migration during peripheral nerve regeneration (By similarity) | |
| Cellular Location Cytoplasm, cytoskeleton (By similarity). Cytoplasm, myofibril (By similarity). Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle) (By similarity) | |
| Tissue Location High-molecular-weight caldesmon (isoform 1) is predominantly expressed in smooth muscles, whereas low-molecular- weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart | |
CALD1 Antibody (Center) - Related products
AP6609c: CALD1 Antibody (Center)
RI10749: CALD1 predesign siRNA
DC07351: Human CALD1 cDNA Clone
LY11581a: CALD1 Over-expression Lysate
BP6609c: CALD1 Antibody (Center) Blocking Peptide
AJ1117a: Caldesmon Antibody (CaM)
AJ1117b: Caldesmon Antibody (CaM)
CALD1 Antibody (Center) - Application data
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Western blot analysis of CALD1 antibody (Center) (Cat. #AP6609c) in A2058 cell line lysates (35ug/lane). CALD1 (arrow) was detected using the purified Pab.
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Formalin-fixed and paraffin-embedded human lung carcinoma with CALD1 Antibody (Center), which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated.
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Flow cytometric analysis of NCI-H292 cells using CALD1 Antibody (Center)(bottom histogram) compared to a negative control cell (top histogram). FITC-conjugated goat-anti-rabbit secondary antibodies were used for the analysis.
CALD1 Antibody (Center) - Research Areas
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BACKGROUND
CALD1 is a calmodulin- and actin-binding protein that plays an essential role in the regulation of smooth muscle and nonmuscle contraction. The conserved domain of this protein possesses the binding activities to Ca(2+)-calmodulin, actin, tropomyosin, myosin, and phospholipids. This protein is a potent inhibitor of the actin-tropomyosin activated myosin MgATPase, and serves as a mediating factor for Ca(2+)-dependent inhibition of smooth muscle contraction.
REFERENCES
Yoshio,T., FEBS Lett. 581 (20), 3777-3782 (2007) Mani,R.S., Biochemistry 31 (47), 11896-11901 (1992)
