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Human Polyclonal SPTA1 Primary Antibody für WB - ABIN6148401
Talhouarne, Gall: 7SL RNA in vertebrate red blood cells. in RNA (New York, N.Y.) 2018
These findings reveal spectrin (alpha/beta) / ankyrin B cytoskeletal and signaling proteins as key regulators of T-type calcium channels expressed in the nervous system.
This study demonstrates that the FGF19-SHP-LSD1 axis maintains homeostasis by suppressing unnecessary autophagic breakdown of cellular components, including lipids, under nutrient-rich postprandial conditions.
a new function for spectrins in the stability of invadosomes and the coupling between actin regulation and ECM degradation
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.
organization of a spectrin-like cytoskeleton is associated with keratinocyte differentiation, and cytoskeleton disruption is mediated by either PKCdelta(Thr505) phosphorylation associated with phosphorylated adducin or due to reduction of endogenous adducin
Results of this study provide evidence for a role for spectrin in different steps of megakaryocyte development through its participation in the formation of invaginated membranes and in the maintenance of proplatelet structure.
Analysis of 3 new alleles reveals previously unknown consequences of red blood cell (RBC) spectrin deficiency, resulting in markedly reduced RBC membrane spectrin content, decreased band 3, and absent beta-adducin.
Murine recessive hereditary spherocytosis, sph/sph, is caused by a mutation in the erythroid alpha-spectrin gene.
a novel HE case with a His54Pro mutation in the SPTA1 gene was reported. The results suggested that the His54Pro mutation influenced the role of erythrocyte membrane proteins without reducing its level of expression.
A novel SPTA1 mutation (H54P) was identified in a case of hereditary elliptocytosis.
The authors show that SUB1-mediated processing of MSP1 is important for parasite viability, the processing modifies the secondary structure of MSP1 and activates its capacity to bind spectrin.
The authors demonstrate that the initial vacuolar membrane around internalized Babesia divergens is formed from protein and lipid components of the red blood cells plasma membrane, including band 3, glycophorin A and spectrin.
Case Report: severe hemolytic jaundice and a phenotype of hereditary spherocytosis due alpha-spectrin mutations.
In this review, we summarize the state of knowledge about interactions between spectrin and membrane lipids
A novel exon 2 alpha spectrin mutation is identified in two families of European ancestry with hereditary pyropoikilocytosis.
The heterozygous c.121C>T mutation of SPTA1 gene induces an amino acid change p.Arg41Trp in the alpha1 domain of the alpha-spectrin protein.
Data show that transcription cofactor TAF3 is required for transcription of the alpha spectrin SPTA1 gene.
The common hereditary elliptocytosis-associated alpha-spectrin leucine260proline mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation.
The unusually slow, two-state kinetics of spectrin assembly in solution, was investigated.
In this review, we summarize recent findings concerning structure and function of spectrin together with its possible role in pathology.
These data further suggest that residues 44 and 53, which are key players in the nucleation-condensation mechanism of folding, are also important triggers of the aggregation process.
analysis of glycosylation of erythrocyte spectrin and its modification in visceral leishmaniasis
Further studies involving siRNA-mediated knockdowns of spectrin, adducin, or p4.1 revealed that those proteins are needed for efficient docking of enterohaemorrhagic Escherichia coli to host cells.
Results suggest that it is possible for cellular proteins to differentially associate with the C-termini of different beta-spectrin isoforms to regulate alpha- and beta-spectrin association to form functional spectrin tetramers.
lipid rafts are associated with the spectrin skeleton in human erythrocytes
The data show that the alpha-spectrin EF domain greatly amplifies the function of the beta-spectrin actin-binding domain in forming the spectrin-actin-4.1R complex.
The functional roles of residues 21-43 and 55-59 in the alpha-spectrin N-terminal region in forming tetramers were determined;mutations may also introduce abnormalities to erythrocytes.
Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is a tetramer made up of alpha-beta dimers linked in a head-to-head arrangement. This gene is one member of a family of alpha-spectrin genes. The encoded protein is primarily composed of 22 spectrin repeats which are involved in dimer formation. It forms weaker tetramer interactions than non-erythrocytic alpha spectrin, which may increase the plasma membrane elasticity and deformability of red blood cells. Mutations in this gene result in a variety of hereditary red blood cell disorders, including elliptocytosis type 2, pyropoikilocytosis, and spherocytic hemolytic anemia.
erythroid spectrin alpha
, spectrin alpha chain, erythrocyte
, alpha-spectrin 1, erythroid
, erythroid alpha-spectrin
, hemolytic anemia
, neuroscience mutagenesis facility, 4
, spectrin alpha 1
, spectrin alpha chain, erythrocytic 1
, alpha-I spectrin