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Recombinant Human Spectrin beta chain, erythrocyte (SPTB), partial

  • 中文名称:
    人SPTB重组蛋白
  • 货号:
    CSB-YP022634HU
  • 规格:
  • 来源:
    Yeast
  • 其他:
  • 中文名称:
    人SPTB重组蛋白
  • 货号:
    CSB-EP022634HU
  • 规格:
  • 来源:
    E.coli
  • 其他:
  • 中文名称:
    人SPTB重组蛋白
  • 货号:
    CSB-EP022634HU-B
  • 规格:
  • 来源:
    E.coli
  • 共轭:
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他:
  • 中文名称:
    人SPTB重组蛋白
  • 货号:
    CSB-BP022634HU
  • 规格:
  • 来源:
    Baculovirus
  • 其他:
  • 中文名称:
    人SPTB重组蛋白
  • 货号:
    CSB-MP022634HU
  • 规格:
  • 来源:
    Mammalian cell
  • 其他:

产品详情

  • 纯度:
    >85% (SDS-PAGE)
  • 基因名:
    SPTB
  • Uniprot No.:
  • 别名:
    Beta I spectrin; Beta spectrin; Beta-I spectrin; EL3; erythrocyte; HS2; HSpTB1; Membrane cytoskeletal protein; Spectrin beta; Spectrin beta chain; Spectrin beta chain erythrocyte; Spectrin beta erythrocytic (includes spherocytosis clinical type I); Spectrin beta erythrocytic; SPH2; sptB; SPTB1; SPTB1_HUMAN
  • 种属:
    Homo sapiens (Human)
  • 蛋白长度:
    Partial
  • 蛋白标签:
    Tag type will be determined during the manufacturing process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 产品提供形式:
    Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 复溶:
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 储存条件:
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期:
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 货期:
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事项:
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet :
    Please contact us to get it.

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. two sex-specific loci(SPTB in females and IZUMO3 in males), yielding associations that were particularly strong at a specific skeletal site, were identified. PMID: 28181694
    2. Using Next-Generation sequencing, we identified the causative genetic mutations in fifteen patients with clinically suspected hereditary elliptocytosis and hereditary pyropoikilocytosis and correlated the identified mutations with the clinical phenotype and ektacytometry profile. PMID: 27667160
    3. Targeted next generation sequencing identifies a novel beta-spectrin gene mutation A2059P in two Omani children with hereditary pyropoikilocytosis PMID: 28699249
    4. Mutational characteristics of ANK1 and SPTB genes in Korean hereditary spherocytosis have been described. PMID: 26830532
    5. a new mutation in the SPTB gene (466insG) leading to a frameshift and a premature stop codon 29 codons downstream in the region encoding the C-terminal part of the dimerization domain; instability of mutant mRNA results in spectrin deficiency and clinically moderate to serious hereditary spherocytosis PMID: 27709257
    6. A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration. PMID: 22360420
    7. Data postulate that direct interactions between spectrin ankBDn and PE-rich domains play an important role in stabilizing the structure of the spectrin-based membrane skeleton. PMID: 21738695
    8. through the use of an ATP-driven phospholipid translocase (flippase), erythrocytes have evolved a protective mechanism against spectrin glycation and thus maintain their optimal membrane function during their long circulatory life span PMID: 20724481
    9. CD45 lateral mobility is regulated by the spectrin-ankyrin cytoskeleton of T cells PMID: 20164196
    10. Important region in the beta-spectrin C-terminus for association with the alpha chain and for spectrin tetramer formation is defined. PMID: 12038451
    11. The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production PMID: 12354383
    12. the repeats of five human beta-spectrins have been analysed PMID: 12655374
    13. This study identifies the precise sites of all significant phosphorylation events on beta-spectrin and has determined that these phosphorylation events apparently occur in a tightly regulated sequential order. PMID: 15065869
    14. Binding sites for both protein 4.1R and actin are located in both of the beta I-spectrin calponin homology domains, (CH1 and CH2). PMID: 16060676
    15. analysis of conformational stabilities of the structural repeats of erythroid spectrin PMID: 16476728
    16. The results indicate that the whole ankyrin-sensitive lipid-binding site of beta-spectrin exhibits a helical conformation revealing a distinct 3(10)-helix contribution at its N-terminus. PMID: 17520478
    17. The spectrin tetramer can be modeled as a soft polymer with a unique flat force-extension profile over the range of biologically important lengths. PMID: 18202182
    18. The structure of the ankyrin ZU5 domain shows a novel structure containing a beta core. PMID: 19141864
    19. The putative coupling of flexibility and ligand binding suggests a mechanism by which spectrin might participate in mechanosensory regulation. PMID: 19168783
    20. DNA analysis of SPTB in hereditary spherocytosis subjects with decreased SPTB mRNA levels revealed the presence of 5 previously undescribed mutations: R1756X, 781delT and IVS22nt-4G>A, 1502insA & IVS20nt-2A>G PMID: 19538529

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  • 相关疾病:
    Elliptocytosis 3 (EL3); Spherocytosis 2 (SPH2)
  • 亚细胞定位:
    Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
  • 蛋白家族:
    Spectrin family
  • 数据库链接:

    HGNC: 11274

    OMIM: 182870

    KEGG: hsa:6710

    STRING: 9606.ENSP00000374372

    UniGene: Hs.417303