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SPTA1 Antibody

  • 货号：
    CSB-PA966552
  • 规格：
    ￥880
  • 其他：

产品详情

  • 产品名称：
    Rabbit anti-Homo sapiens (Human) SPTA1 Polyclonal antibody
  • Uniprot No.：
    P02549
  • 基因名：
  • 别名：
    Alpha I spectrin antibody; EL 2 antibody; EL2 antibody; Elliptocytosis 2 antibody; Elliptocytosis2 antibody; Erythrocyte alpha spectrin antibody; erythrocyte antibody; Erythroid alpha spectrin antibody; Erythroid alpha-spectrin antibody; Erythroid spectrin alpha antibody; HPP antibody; HS3 antibody; Spectrin alpha chain antibody; Spectrin alpha chain erythrocyte antibody; Spectrin alpha erythrocytic 1 antibody; SPH3 antibody; SPTA 1 antibody; SPTA antibody; SPTA1 antibody; SPTA1_HUMAN antibody
  • 宿主：
    Rabbit
  • 反应种属：
    Human, Mouse
  • 免疫原：
    Synthetic peptide of Human SPTA1
  • 免疫原种属：
    Homo sapiens (Human)
  • 标记方式：
    Non-conjugated
  • 克隆类型：
    Polyclonal
  • 抗体亚型：
    IgG
  • 纯化方式：
    Antigen Affinity Purified
  • 浓度：
    It differs from different batches. Please contact us to confirm it.
  • 保存缓冲液：
    PBS with 0.05% sodium azide, 40% glycerol, pH7.4
  • 产品提供形式：
    Liquid
  • 应用范围：
    ELISA, WB, IHC
  • 推荐稀释比：
    Application Recommended Dilution
    WB 1:200-1:1000
    IHC 1:25-1:100
  • Protocols：
  • 储存条件：
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 货期：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

产品评价

靶点详情

  • 功能：
    Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
  • 基因功能参考文献：
    1. 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. PMID: 29484404
    2. A novel SPTA1 mutation (H54P) was identified in a case of hereditary elliptocytosis. PMID: 28694211
    3. The s 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. PMID: 26468747
    4. The s 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. PMID: 25628009
    5. a new function for spectrins in the stability of invadosomes and the coupling between actin regulation and ECM degradation PMID: 25830635
    6. Case Report: severe hemolytic jaundice and a phenotype of hereditary spherocytosis due alpha-spectrin mutations. PMID: 25277063
    7. In this review, we summarize the state of knowledge about interactions between spectrin and membrane lipids PMID: 24569979
    8. A novel exon 2 alpha spectrin mutation is identified in two families of European ancestry with hereditary pyropoikilocytosis. PMID: 24077844
    9. 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. PMID: 24003435
    10. Data show that transcription cofactor TAF3 is required for transcription of the alpha spectrin SPTA1 gene. PMID: 23935956
    11. The common hereditary elliptocytosis-associated alpha-spectrin leucine260proline mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. PMID: 23974198
    12. The unusually slow, two-state kinetics of spectrin assembly in solution, was investigated. PMID: 23200054
    13. In this review, we summarize recent findings concerning structure and function of spectrin together with its possible role in pathology. PMID: 23373410
    14. 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. PMID: 22727745
    15. analysis of glycosylation of erythrocyte spectrin and its modification in visceral leishmaniasis PMID: 22164239
    16. 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. PMID: 22197999
    17. 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. PMID: 21412925
    18. lipid rafts are associated with the spectrin skeleton in human erythrocytes PMID: 20807499
    19. 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. PMID: 20585040
    20. 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. PMID: 19747366
    21. identification and characterization of the gene promoter; requires GATA-1- and NF-E2-binding proteins to direct high level expression in erythroid cells in vitro. PMID: 12196550
    22. Quantitative analysis of erythrocyte membrane proteins revealed increase in alpha-spectrin from patients with homozygous and heterozygous forms of beta-thalassemia. PMID: 15310273
    23. a region 3' of the alpha-spectrin core promoter contains a GATA-1-dependent positive regulatory element that is required in its proper genomic orientation PMID: 15456760
    24. analysis of erythroid alpha and beta spectrin chaperone activity and prodan binding PMID: 15492010
    25. Ubiquitination of alpha-spectrin does not regulate heterodimer formation. PMID: 15795915
    26. splicing mutation in hereditary pyropoikilocytosis kindred PMID: 16150946
    27. We found that cysteine 2071 & cysteine 2100 are critical for alpha-spectrin (2005-2415) E2/E3 activity; also demonstrated that both Cys2071 & Cys2100 are capable of transferring ubiquitin from an E1 enzyme to target sites within alpha-spectrin (2005-2415) PMID: 16171554
    28. the interaction of the alphaII-spectrin SH3 domain with EVL PMID: 16336193
    29. These results suggest a role for spectrin in providing a dynamic and reversible signaling platform to the specific domains of the plasma membrane in response to stimulation of GPCR. PMID: 16551696
    30. Results provide evidence that protein degradation of alphaII-spectrin is a reliable marker of severe traumatic brain injury (TBI) in humans and that both necrotic and apoptotic cell death mechanisms are activated in humans following a severe TBI. PMID: 16841024
    31. REVIEW: Culture studies of Plasmodium falciparum in elliptocytes bearing such elliptocytogenic alleles of spectrin showed that these alleles are supplementary genetic factors of malaria resistance PMID: 17414207
    32. The absence of particular spectrin isoforms may correlate with transformation or aggressive biologic behavior for some lymphoma subtypes. PMID: 17885671
    33. analysis of the conformational change of erythroid alpha-spectrin at the tetramerization site upon binding beta-spectrin PMID: 17905835
    34. This model supports the hypothesis that initial docking of the correct alpha and beta repeats from among many very similar repeats in both subunits is driven primarily by long range electrostatic interactions. PMID: 17977835
    35. All alpha0 HE/HPP mutations studied here appear to exert their destabilizing effects through molecular recognition rather than structural mechanisms. PMID: 18218854
    36. Erythrocytes from most jereditary pyropoikilocytosis (inherited hemolytic anemia) exhibit abnormalities in the alpha-spectrin gene. PMID: 18815189
    37. exon 1' and intron 1' are excellent candidate regions for mutations in patients with spectrin-linked hemolytic anemia PMID: 19008453
    38. The L49F mutation in alpha erythroid spectrin leads to an unstable triple helical bundle of alpha beta-spectrin partial domains, and thus unstable tetramers. PMID: 19593814

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  • 相关疾病：
    Elliptocytosis 2 (EL2); Hereditary pyropoikilocytosis (HPP); Spherocytosis 3 (SPH3)
  • 亚细胞定位：
    Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
  • 蛋白家族：
    Spectrin family
  • 数据库链接：

    HGNC: 11272

    OMIM: 130600

    KEGG: hsa:6708

    STRING: 9606.ENSP00000357130

    UniGene: Hs.119825