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Human ANKRD1 Protein expressed in Escherichia coli (E. coli) - ABIN1098397
Chu, Burns, Swerlick, Presky: Identification and characterization of a novel cytokine-inducible nuclear protein from human endothelial cells. in The Journal of biological chemistry 1995
Show all 2 references for ABIN1098397
These data suggest that hepatitis C virus coopts ANKRD1 for its own propagation and up-regulation of ANKRD1 may contribute to hepatitis C virus-mediated liver pathogenesis.
To the Ankrd1, it is not responsive to the cardiotoxic drug Doxorubicin, suggesting that different mechanisms govern their expression in cardiac cells.
The association of ANKRD1 with antiapoptotic response suggests its role as myocyte survival factor during late stage heart disease, warranting further studies on ANKRD1 during end-stage heart failure.
Report structure activity relationships for ANKRD1.
ANKRD1 has a significant role in the regulation of apoptosis in human ovarian cancer cells
Augmented CARP (show CA8 Proteins) expression may be a common molecular event in failing hearts regardless of cardiomyopathic aetiology.
Report impact of ANKRD1 mutations associated with hypertrophic cardiomyopathy on contraction parameters of engineered heart tissue.
the 26S proteasome (show Psmd4 Proteins) is the dominant regulator of Ankrd1/CARP degradation, and that Ankrd1/CARP half-life is significantly longer in cardiomyocytes (h) than endothelial cells (min).
Ankrd1 and desmin (show DES Proteins) may play important roles in airway smooth muscle cell homeostasis.
CARP (show CA8 Proteins) and its regulator calpain 3 (show CAPN3 Proteins) appear to occupy a central position in the important cell fate-governing NF-kappaB (show NFKB1 Proteins) pathway in skeletal muscle
Overexpression of Ankrd1 exacerbates pathological cardiac remodeling through the enhancement of cytosolic translocation of CARP and up-regulation of calcineurin (show PPP3CA Proteins).
ANKRD1 modulates inflammatory responses in myoblasts through feedback inhibition of NF-kappaB (show NFKB1 Proteins) signaling activity.
ANKRD1 is important for the proper interaction of fibroblasts with a compliant collagenous matrix both in vitro and in vivo
Overexpression of Ankrd1 exacerbates pathological cardiac dysfunction through enhancement of cardiomyocyte apoptosis mediated by the up-regulation of p53 (show TP53 Proteins).
CARP, Ankrd2 (show ANKRD2 Proteins), and DARP (show Ankrd23 Proteins) are not essential for normal cardiac development and function at basal conditions and in response to mechanical pressure overload.
ANKRD1, in association with factors such as nucleolin (show NCL Proteins), represses MMP13 (show MMP13 Proteins) transcription. Ankrd1 deletion additionally relieved MMP10 (show MMP10 Proteins) transcriptional repression
CARP attenuates cardiac hypertrophy, in which the ERK (show EPHB2 Proteins) and TGF-beta (show TGFB1 Proteins) pathways may be involved. Our findings highlight the significance of CARP as an anti-hypertrophic factor in therapy of cardiac hypertrophy
CARP is expressed during adulthood in response to neurological stimuli, such as kainic acid-induced seizures.
Data show that CARP specific expressed in mouse heart and mainly localized in the nucleus in rat cardiac primary cells.
CARP mRNA expression is detected in an atherosclerotic lesion at the aortic valves of an APOE (show APOE Proteins)*3-Leiden mouse after 16 weeks of Western-type diet and is expressed in an intimal smooth muscle cell-rich lesion induced by carotid artery ligation.
Expression analysis in porcine satellite cells showed that CARP and ANKRD2 (show ANKRD2 Proteins) were induced in differentiated porcine satellite cells, suggesting a role of them in myogenic differentiation.
endogenous ANKRD1 and calsequestrin are co-enriched in piglet cardiac Purkinje cells
CAPZB (show CAPZB Proteins), ANKRD1, and CTBP2 (show CTBP2 Proteins) are promoted as candidate genes for meat quality that provide a link between signal pathways.
The protein encoded by this gene is localized to the nucleus of endothelial cells and is induced by IL-1 and TNF-alpha stimulation. Studies in rat cardiomyocytes suggest that this gene functions as a transcription factor. Interactions between this protein and the sarcomeric proteins myopalladin and titin suggest that it may also be involved in the myofibrillar stretch-sensor system.
ankyrin repeat domain 1 (cardiac muscle)
, cardiac ankyrin repeat protein
, ankyrin repeat domain-containing protein 1
, ankyrin-like repeat protein
, cardiac adriamycin-responsive protein
, cardiac responsive adriamycin protein
, muscle ankyrin repeat protein
, cytokine-inducible gene C-193 protein
, cytokine-inducible nuclear protein
, liver ankyrin repeat domain 1