在线日韩日本国产亚洲丨少妇伦子伦情品无吗丨欧美性猛交xxxx免费看蜜桃丨精品人妻系列无码一区二区三区丨亚洲精品无码不卡在线播放

Your Good Partner in Biology Research

ALAS2 Antibody

  • 中文名稱:
    ALAS2兔多克隆抗體
  • 貨號:
    CSB-PA001560LA01HU
  • 規格:
    ¥440
  • 圖片:
    • Western blot
      All lanes: ALAS2 antibody at 6µg/ml + K562 whole cell lysate
      Secondary
      Goat polyclonal to rabbit IgG at 1/10000 dilution
      Predicted band size: 65, 61, 50, 64 kDa
      Observed band size: 65 kDa
    • Immunohistochemistry of paraffin-embedded human liver tissue using CSB-PA001560LA01HU at dilution of 1:100
    • Immunohistochemistry of paraffin-embedded human thyroid tissue using CSB-PA001560LA01HU at dilution of 1:100
  • 其他:

產品詳情

  • 產品名稱:
    Rabbit anti-Homo sapiens (Human) ALAS2 Polyclonal antibody
  • Uniprot No.:
  • 基因名:
    ALAS2
  • 別名:
    5 @aminolevulinate synthase erythroid specific antibody; 5 aminolevulinate synthase 2 antibody; 5 aminolevulinate synthase 5 aminolevulinate synthase 2 antibody; 5 aminolevulinate synthase erythroid specific mitochondrial antibody; 5 aminolevulinic acid synthase 2 antibody; 5 aminolevulinic acid synthase antibody; 5-aminolevulinate synthase antibody; 5-aminolevulinic acid synthase 2 antibody; Alas 2 antibody; ALAS antibody; ALAS E antibody; ALAS; erythroid antibody; ALAS-E antibody; Alas2 antibody; ALASE antibody; Aminolevulinate delta synthase 2 antibody; Aminolevulinic acid synthase 2; erythroid antibody; ANH1 antibody; ASB antibody; Delta ALA synthase 2 antibody; Delta ALA synthetase antibody; Delta aminolevulinate synthase 2 antibody; Delta aminolevulinate synthase antibody; Delta-ALA synthase 2 antibody; Delta-aminolevulinate synthase 2 antibody; Erythroid specific ALAS antibody; erythroid-specific antibody; FLJ93603 antibody; HEM0_HUMAN antibody; mitochondrial antibody; OTTHUMP00000023388 antibody; OTTHUMP00000023389 antibody; OTTMUSP00000020679 antibody; RP23-338A17.1 antibody; SIDBA1 antibody; XLDPP antibody; XLEPP antibody; XLSA antibody
  • 宿主:
    Rabbit
  • 反應種屬:
    Human
  • 免疫原:
    Recombinant Human 5-aminolevulinate synthase, erythroid-specific, mitochondrial protein (50-587AA)
  • 免疫原種屬:
    Homo sapiens (Human)
  • 標記方式:
    Non-conjugated

    本頁面中的產品,ALAS2 Antibody (CSB-PA001560LA01HU),的標記方式是Non-conjugated。對于ALAS2 Antibody,我們還提供其他標記。見下表:

    可提供標記
    標記方式 貨號 產品名稱 應用
    HRP CSB-PA001560LB01HU ALAS2 Antibody, HRP conjugated ELISA
    FITC CSB-PA001560LC01HU ALAS2 Antibody, FITC conjugated
    Biotin CSB-PA001560LD01HU ALAS2 Antibody, Biotin conjugated ELISA
  • 克隆類型:
    Polyclonal
  • 抗體亞型:
    IgG
  • 純化方式:
    >95%, Protein G purified
  • 濃度:
    It differs from different batches. Please contact us to confirm it.
  • 保存緩沖液:
    Preservative: 0.03% Proclin 300
    Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
  • 產品提供形式:
    Liquid
  • 應用范圍:
    ELISA, WB, IHC
  • 推薦稀釋比:
    Application Recommended Dilution
    WB 1:1000-1:5000
    IHC 1:20-1:200
  • Protocols:
  • 儲存條件:
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 貨期:
    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.
  • 用途:
    For Research Use Only. Not for use in diagnostic or therapeutic procedures.

產品評價

靶點詳情

  • 基因功能參考文獻:
    1. we report that the dynamics of ALAS2 active site loop is anti-correlated with the dynamics of the C-terminal tail and that this anti-correlation can represent a molecular basis for the functional and dynamic asymmetry of the ALAS2 homodimer. PMID: 29958424
    2. report confirms the considerable variability in manifestations among patients with ALAS2 or SLC25A38 mutations and draws attention to differences in the assessment and the monitoring of iron overload and its complications PMID: 28772256
    3. A novel ALAS2 missense mutation in exon 9 affects the enzymatic activity of ALAS2 by affecting its interaction with the cofactor pyridoxal 5'-phosphate in X-linked sideroblastic anemia. PMID: 28667034
    4. a case of X-linked sideroblastic anemia caused by a novel homozygous deletional mutation in exon 10 of ALAS2 gene is presented PMID: 28731922
    5. int-1-GATA site should be examined in patients with XLSA in clinical settings when no known mutation is found in ALAS2 exons. PMID: 28123038
    6. From pH jump experiments, comparable rates for the denaturation of the tertiary structure and PLP-microenvironment were discerned, indicating that the catalytic active site geometry strongly depends on the stable tertiary structural organization. Lastly, we demonstrate that partially folded ALAS tends to self-associate into higher oligomeric species at moderate GuHCl concentrations. PMID: 27751851
    7. data indicate that the X-linked protoporphyria variants possess enhanced ALAS activity and ALA dissociation rates, as well as distinct structural properties from those of wild-type hALAS PMID: 26300302
    8. In this article we add a novel mutation to the previously described 61 different ALAS2 mutations identified in X-linked sideroblastic anaemia patients. PMID: 24829177
    9. the primary deficiency in ferrochelatase leads to a secondary increase in ALAS2 expression. PMID: 25179834
    10. The ALAS2 Y365C mutation impairs pyridoxal 5'-phosphate binding to ALAS2, destabilizing the enzyme. X inactivation was not highly skewed in WBC from affected women. This X-linked dominant mutation perturbs erythropoiesis via cell-nonautonomous effects. PMID: 25705881
    11. the 130-base pair enhancer region located in the first intron of the ALAS2 gene should be examined in patients with congenital sideroblastic anemia in whom the gene responsible is unknown. PMID: 23935018
    12. 5 families with X-linked sideroblastic anemia had mutations in a GATA transcription factor binding site located in a transcriptional enhancer element in intron 1 of the ALAS2 gene. PMID: 24166784
    13. Loss-of-function FECH and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria and x-linked protoporphyria in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria. PMID: 23364466
    14. ALAS2 gain-of-function mutations increas the specific activity (DeltaAT, DeltaAGTG and p.Q548X) or stability (DeltaG) of the enzyme, thereby leading to the increased erythroid protoporphyrin accumulation causing X-linked protoporphyria. PMID: 23348515
    15. A large gain-of-function domain within the C-terminus of ALAS2 is associated with X-linked dominant protoporphyria. PMID: 23263862
    16. Late-onset photosensitivity was caused by ALAS2 mutation in a family with dominant protoporphyria. PMID: 23223129
    17. X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the beta-subunit of succinyl-CoA synthetase (SUCLA2). PMID: 22740690
    18. the C-terminal region of ALAS2 protein may function as an intrinsic modifier that suppresses catalytic activity and increases the degradation of its protein, each function of which is enhanced by the Met567Ile mutation and Val562Ala mutation, respectively PMID: 22269113
    19. Data suggest that ALAS2 gene mutations should be considered not only as causative of X-linked sideroblastic anemia (XLSA) and XLDPP but may also modulate gene function in other erythropoietic disorders. PMID: 21653323
    20. identification of five probands with sideroblastic anemia and ALAS2 R452S (due to SNP); all were African-American males; all presented with moderate anemia; the four adults presented with iron overload [a multi-case report from the United States] PMID: 21800356
    21. Thirteen different ALAS2 mutations were identified in 16 out of 29 probands with sideroblastic anemia. PMID: 21309041
    22. We found the previously published R452H and R452C ALAS2 mutations in 3 patients with X-linked sideroblastic anemia PMID: 21252495
    23. HIF1-mediated ALAS2 upregulation promotes erythropoiesis to satisfy the needs of an organism under hypoxic conditions. PMID: 21207956
    24. About 4% of unrelated EPP patients have X-linked dominant protoporphyria (MIM 300752) caused by gain-of-function mutations in the ALAS2 gene leading to an increased erythroid heme biosynthesis & protoporphyrin accumulation. Review. PMID: 20850938
    25. Seven ALAS2 mutations were detected in eight sporadic CSA cases, two being novel: V301A in a male patient and R517G in a female patient PMID: 19731322
    26. A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia. PMID: 12031592
    27. A C to G transversion at nucleotide -206 from the transcription start site was found in the proximal promoter region of ALAS2 in X-linked sideroblastic anemia. The region of the mutation may bind a novel and important erythroid regulatory element. PMID: 12663458
    28. the major splice isoform of ALAS2 is functional in vivo and could significantly contribute to erythroid heme biosynthesis and hemoglobin formation PMID: 14643893
    29. there is nucleotide variation at Msn and Alas2 on the X chromosome PMID: 15166166
    30. sequence identity of ALAS from Rhodobacter capsulatus and human eALAS is 49% PMID: 16121195
    31. ALAS2 mutations might contribute to more severe iron loading in persons with primary hemochromatosis. PMID: 16446107
    32. upon the NaBu stimulation, binding of Sp1 protein to ALAS2 promoter increased significantly, with concurrent increases in acetylation level of histone H3 and dimethylation level of H3-Lysine4 at ALAS2 promoter PMID: 18555711
    33. An impact of ALAD2 on blood lead levels or hemoglobin was not seen in Romanian women from a lead-contaminated region. PMID: 18569569
    34. gain-of-function mutations in ALAS2 cause a previously unrecognized form of porphyria, X-linked dominant protoporphyria, characterized biochemically by a high proportion of zinc-protoporphyrin in erythrocytes PMID: 18760763
    35. Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G. PMID: 19066423
    36. Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling. PMID: 19187226

    顯示更多

    收起更多

  • 相關疾病:
    Anemia, sideroblastic, 1 (SIDBA1); Erythropoietic protoporphyria, X-linked dominant (XLDPT)
  • 亞細胞定位:
    Mitochondrion matrix.
  • 蛋白家族:
    Class-II pyridoxal-phosphate-dependent aminotransferase family
  • 組織特異性:
    Erythroid specific.
  • 數據庫鏈接:

    HGNC: 397

    OMIM: 300751

    KEGG: hsa:212

    STRING: 9606.ENSP00000332369

    UniGene: Hs.522666



主站蜘蛛池模板: 翘臀后进少妇大白嫩屁股| 永久免费无码日韩视频| 国产精品亚洲精品日韩已满| 国精品人妻无码一区免费视频电影| 精品国产乱码久久久久久下载| 少妇无码av无码去区钱| 天堂…中文在线最新版在线| 国产日产亚洲系列最新| 伊人久久精品在热线热| 中文字字幕在线乱码视频| 亚洲人成伊人成综合网久久久| 一本一道人人妻人人妻αv| 亚洲gv猛男gv无码男同| 亚洲国产精品无码7777一线| 日韩精品久久久免费观看 | 日本无码欧美一区精品久久| 欧美成人一区二区三区在线视频 | 福利姬国产精品一区在线| 国产精品久久久影视青草| 国产色视频自在线观看| 亚洲国产精品久久久久秋霞小说| 国产高清在线精品一区下载| 精品久久人人爽天天玩人人妻| 国产好爽…又高潮了毛片| 国产午夜亚洲精品一区| 日韩亚洲欧美中文高清在线| 欧美激情一区二区| 国产午夜精品一区二区三区老| 潮喷大喷水系列无码久久精品| 免费无码国产欧美久久18| 又粗又大又硬又长又爽| 久久综合九色综合97婷婷| 欧美人与动牲交免费观看网| 亚洲人成网7777777国产| 无码中文字幕日韩专区| 日韩精品无码一区二区忘忧草| 少妇激情作爱视频| 强开小婷嫩苞又嫩又紧视频| 日本孕妇潮喷高潮视频| 伊人久久大香线蕉精品| 欧美老熟妇乱xxxxx|