MW 764.7 Da, Purity >97%. Selective Ca2+ chelator. Cell-permeable analog of BAPTA (ab120449). Useful for manipulation of intracellular free Ca2+ levels. Shows varied biological activity. Blocks hKv1.5, Kv11.1 (hERG) and hKv1.3 channels (Ki values are 1.23, 1.30 and 1.45 μM, respectively).
AI838772, AW493413, FLJ11090, Hypothetical protein FLJ35932, MGC104252, MGC112732, RP24-311F12.2, SCAN1, STK33_HUMAN, Serine threonine kinase 33, Serine/threonine kinase 33, Serine/threonine-protein kinase 33, TYDP, TYDP1_HUMAN, Tyr-DNA phosphodiesterase 1, Tyrosyl-DNA phosphodiesterase 1
MW 764.7 Da, Purity >97%. Selective Ca2+ chelator. Cell-permeable analog of BAPTA (ab120449). Useful for manipulation of intracellular free Ca2+ levels. Shows varied biological activity. Blocks hKv1.5, Kv11.1 (hERG) and hKv1.3 channels (Ki values are 1.23, 1.30 and 1.45 μM, respectively).
Soluble in DMSO to 100 mM.
Selective Ca2+ chelator. Cell-permeable analog of BAPTA (ab120449). Useful for manipulation of intracellular free Ca2+ levels. Shows varied biological activity. Blocks hKv1.5, Kv11.1 (hERG) and hKv1.3 channels (Ki values are 1.23, 1.30 and 1.45 μM, respectively).
TDP1 also known as Tyrosyl-DNA Phosphodiesterase 1 or TDP1p is an enzyme that plays an important role in DNA repair. It has a molecular mass of approximately 67 kDa and is expressed ubiquitously across various human tissues suggesting its fundamental role in maintaining genomic stability. Mechanically TDP1 acts by cleaving the phosphodiester bond between a tyrosine residue and a DNA 3' terminus which is important in resolving protein-DNA complexes that result from DNA damage.
This enzyme is indispensable in the repair of topoisomerase I-mediated DNA damage participating as an important player in the DNA repair machinery. TDP1 works within the context of a complex involving other repair proteins ensuring the removal of DNA-protein cross-links that could otherwise lead to cell death if left unrepaired. This activity highlights its role in genomic stability and cell viability.
TDP1 finds its place within the DNA single-strand break repair and the DNA damage response pathways. Its function is closely associated with other proteins such as XRCC1 which enhances the stability and efficiency of the DNA repair process and PARP1 which directs the cell's response to DNA damage. These interactions highlight TDP1's role in safeguarding genetic information by enabling precise and effective repair mechanisms.
TDP1 is notably implicated in neurodegenerative conditions such as Spinocerebellar Ataxia with Axonal Neuropathy (SCAN1) demonstrating how critical its proper function is for neuronal survival. Mutations or dysregulation in TDP1 have also been linked to heightened sensitivity to chemotherapeutic agents indicating potential challenges in cancer treatment. These disease linkages put TDP1 in association with proteins like ATM and BRCA1 which are involved in cellular responses to DNA damage and maintaining genomic integrity.
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2D chemical structure image of ab120503, BAPTA-AM, Ca2+ chelator
Anti-PAI1 antibody ab66705 staining PAI1 in HepG2 cells treated with BAPTA-AM (ab120503), by ICC/IF. Increase in PAI1 expression correlates with increased concentration of BAPTA-AM, as described in literature.
The cells were incubated at 37°C for 4 hours in media containing different concentrations of ab120503 (BAPTA-AM) in DMSO, fixed with 100% methanol for 5 minutes at -20°C and blocked with PBS containing 10% goat serum, 0.3 M glycine, 1% BSA and 0.1% tween for 2h at room temperature. Staining of the treated cells with Anti-PAI1 antibody ab66705 (5 µg/ml) was performed overnight at 4°C in PBS containing 1% BSA and 0.1% tween. A DyLight 488 goat anti-rabbit polyclonal antibody (Goat Anti-Rabbit IgG H&L (DyLight® 488) preadsorbed ab96899) at 1/250 dilution was used as the secondary antibody. Nuclei were counterstained with DAPI and are shown in blue.
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