Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Aberrant DNA methylation (show HELLS Proteins) of ADD2 could be potential screening markers of colorectal cancer.
Study evaluated effects of ADD genetic variability on cognitive functions in a sample of patients with schizophrenia, known to show a wide and heterogeneous neuropsychological deficit and found that ADD2 C1797T polymorphism showed diffuse effects on almost every cognitive domain.
ADD2 and NCX1 (show SLC8A1 Proteins) variants influence the risk and the clinical features of systemic lupus erythematosus and lupus nephritis.
Taken together, these results show that beta-adducin is a pivotal lipid raft-associated protein in PSGL-1 (show SELPLG Proteins)-mediated neutrophil rolling on P-selectin (show SELP Proteins).
chorein interacts with beta-adducin and beta-actin (show ACTB Proteins).
phosphorylation of beta-adducin by GSK3 promotes efficient neurite outgrowth in neurons.
ALPHA AND BETA ADDUCIN POLYMORPHISMS AFFECT DECLINE OF RENAL FUNCTION IN HUMAN IGA NEPHROPATHY.
there was significant heterogeneity between Slavic and Italian subjects in the phenotype-genotype relationships with beta-adducin
Expression of the hypertensive rat or human variant of adducin into normal renal epithelial cells recreates the hypertensive phenotype with higher Na+,K+-ATPase (show ATP1A1 Proteins) activity, mu2 (show AP2M1 Proteins)-subunit hyperphosphorylation, and impaired Na+,K+-ATPase (show ATP1A1 Proteins) endocytosis.
Polymorphisms in the ADD2 and ADD3 (show ADD3 Proteins) genes taken alone were not associated with blood pressure and renin (show REN Proteins) activity
Sez6l2 (show SEZ6L2 Proteins) is one of the auxiliary subunits of the AMPA (show GRIA3 Proteins) receptor and acts as a scaffolding protein to link GluR1 (show GRIA1 Proteins) to ADD. Furthermore, Sez6l2 (show SEZ6L2 Proteins) overexpression upregulates ADD phosphorylation, whereas siRNA-mediated downregulation of Sez612 prevents ADD phosphorylation, suggesting that Sez6l2 (show SEZ6L2 Proteins) modulates AMPA (show GRIA3 Proteins)-ADD signal transduction.
Darpp32 (show PPP1R1B Proteins) interaction with beta-adducin may be the molecular pathway by which environmental changes may rapidly alter responsiveness of striatal neurons involved in the reward system.
Calcium plays a role in regulating the expression and function of beta-adducin to sustain normal organization of the spectrin-based cytoskeleton and the differentiation properties in keratinocytes through the calmodulin/EGFR/cadherin signaling pathway.
study identified novel long-distance upstream non-canonical polyadenylation-regulatory elements that enhance or silence 3'end processing of the Add2 PAS4 (show CD36 Proteins)
mice lacking beta-Adducin fail to assemble new synapses upon enhanced plasticity and exhibit diminished long-term hippocampal memory upon environmental enrichment.
Analysis of 3 new alleles reveals previously unknown consequences of red blood cell (RBC (show CACNA1C Proteins)) spectrin deficiency, resulting in markedly reduced RBC (show CACNA1C Proteins) membrane spectrin content, decreased band 3 (show SLC4A1 Proteins), and absent beta-adducin.
Further analysis based on antibody staining of central and peripheral nerves revealed beta-adducin, septin 2 (show SEPT2 Proteins), and sh3p8 (show SH3GL1 Proteins) as putative paranodal proteins.
beta-Adducin may play an important role in the cellular mechanisms underlying activity-dependent synaptic plasticity associated with learning and memory.
Beta-adducin plays an essential role in the maintenance of erythrocyte shape and membrane stability.
Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. While adducins alpha and gamma are ubiquitously expressed, the expression of adducin beta is restricted to brain and hematopoietic tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Heterodimers consisting of alpha and gamma subunits have also been described. Structurally, each subunit is comprised of two distinct domains. The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Alternatively spliced transcript variants have been described.
adducin 2 (beta)
, erythrocyte adducin subunit beta
, snoRNA MBII-396
, adducin beta