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Rat calmodulin,CAM ELISA Kit

  • 中文名稱:
    大鼠鈣調素(CAM)酶聯免疫試劑盒
  • 貨號:
    CSB-E09753r
  • 規格:
    96T/48T
  • 價格:
    ¥3900/¥2500
  • 其他:

產品詳情

  • 產品描述:
    大鼠鈣調素(CAM)酶聯免疫試劑盒(CSB-E09753r)為雙抗夾心法ELISA試劑盒,定量檢測血清、血漿樣本中的CALM1含量。CALM1編碼鈣調蛋白,在細胞內廣泛存在。它能與鈣離子結合,調節眾多細胞生理過程。研究發現其參與細胞增殖、凋亡、運動等機制。目前圍繞CALM1在疾病發生發展中的作用及潛在治療靶點等方面開展研究,有望為相關疾病治療帶來新方向。試劑盒檢測范圍為15.6 ng/mL-1000 ng/mL,該產品適用于基礎科研領域中對鈣信號通路機制、疾病模型構建及藥物干預效果的評價,例如通過檢測血清或血漿中CAM的動態變化,可探究其在鈣離子依賴性生理病理過程中的調控作用,為細胞信號轉導、神經生物學等研究提供可靠工具。本品僅用于科研,不用于臨床診斷,產品具體參數及操作步驟詳見產品說明書。
  • 別名:
    Calm1 ELISA kit; Calm ELISA kit; Cam ELISA kit; Cam1 ELISA kit; CaMICalmodulin-1 ELISA kit
  • 縮寫:
  • Uniprot No.:
  • 種屬:
    Rattus norvegicus (Rat)
  • 樣本類型:
    serum, plasma
  • 檢測范圍:
    15.6 ng/mL-1000 ng/mL
  • 靈敏度:
    3.9 ng/mL
  • 反應時間:
    1-5h
  • 樣本體積:
    50-100ul
  • 檢測波長:
    450 nm
  • 研究領域:
    Signal Transduction
  • 測定原理:
    quantitative
  • 測定方法:
    Sandwich
  • 精密度:
    Intra-assay Precision (Precision within an assay): CV%<8%
    Three samples of known concentration were tested twenty times on one plate to assess.
    Inter-assay Precision (Precision between assays): CV%<10%
    Three samples of known concentration were tested in twenty assays to assess.
  • 線性度:
    To assess the linearity of the assay, samples were spiked with high concentrations of rat CAM in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
    SampleSerum(n=4)
    1:5Average %88
    Range %85-91
    1:10Average %96
    Range %94-98
    1:20Average %89
    Range %87-90
    1:40Average %104
    Range %101-107
  • 回收率:
    The recovery of rat CAM spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
    Sample TypeAverage % RecoveryRange
    Serum (n=5) 9995-102
    EDTA plasma (n=4)104101-107
  • 標準曲線:
    These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
    ng/mlOD1OD2AverageCorrected
    10002.819 2.836 2.828 2.632
    5002.181 2.101 2.141 1.945
    2501.494 1.475 1.485 1.289
    1250.919 0.935 0.927 0.731
    62.50.588 0.598 0.593 0.397
    31.20.402 0.432 0.417 0.221
    15.60.287 0.275 0.281 0.085
    00.195 0.197 0.196
  • 數據處理:
  • 貨期:
    3-5 working days

產品評價

靶點詳情

  • 功能:
    Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endomplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2.
  • 基因功能參考文獻:
    1. Tau could inhibit the H2O2-induced decrease in CamKII and CaM expression at both the mRNA and protein levels. PMID: 29279520
    2. These results suggest a connection between Ca(2+)-signaling via excitation-contraction coupling and the regulation of STARS-mediated gene expression in muscles. PMID: 27132186
    3. Hydrogen peroxide reduces calmodulin binding to RYR2 in rat cardiomyocytes. PMID: 26092277
    4. Disruption of calmodulin binding to KCNQ2 also impairs enrichment of heteromeric KCNQ2/KCNQ3 channels at the axonal surface by blocking their trafficking from the endoplasmic reticulum to the axon. PMID: 25077630
    5. Study reveals that apoCaM itself prominently regulates both voltage-gated Ca2+ and Na channels; ApoCaM binding to these channels enhances opening several-fold, matching the strongest forms of ion-channel regulation. PMID: 25417111
    6. The molecular events underlying the association between CaM and Kv7.2 and their regulation by Ca(2+), was examined. PMID: 24489773
    7. The study proposes that the structural basis of calcineurin activation by calmodulin is through displacement of the disordered fragment of the autoinhibitory domain which otherwise impedes active site access. PMID: 24018048
    8. Recombinant small (SK2) calcium channel and calmodulin bind with three different stoichiometries that depend on the molar ratio of 2SKp/2CaM in solution. PMID: 24420768
    9. CK2-mediated phosphorylation of calmodulin regulates the M-current, which is tonically regulated by CK2 and PP1 anchored to the KCNQ2 channel complex. PMID: 24627475
    10. GRK5 nuclear translocation downstream of select Gq-activating hypertrophic ligands is a calmodulin-dependent process PMID: 23472081
    11. Structural basis for the association of MAP6 protein with microtubules and its regulation by calmodulin. PMID: 23831686
    12. Data indicate that the two distinct CaM/OLFp complexes existed simultaneously with stable structures. PMID: 22877078
    13. structures of intact calmodulin (CaM)-free and CaM-bound endothelial nitric oxide synthase (eNOS) PMID: 23266515
    14. Sustained Epac activation induces a strong positive inotropic effect relating to enhanced calcium signaling and increased expression of calmodulin. PMID: 22910094
    15. Neurogranin targets calmodulin and lowers the threshold for the induction of long-term potentiation. PMID: 22848456
    16. The crystal structure of a CaM.Orai1-calmodulin binding domain complex, is reported. PMID: 23109337
    17. Cx32 is differentially phosphorylated and exists in a complex with SAP97 and CaM. PMID: 22718765
    18. Calmodulin bound to the first IQ motif is responsible for calcium-dependent regulation of myosin 5a. PMID: 22437832
    19. In PMCA-suppressed lines total CaM increased, and the calm I and calm II genes appeared to be responsible for this effect PMID: 21912933
    20. Calmodulin facilitates endocytosis in an activity-dependent manner. PMID: 22184217
    21. PKC and CaM protein expressions were downregulated in the hippocampus of neonatal rats exposed to lead. PMID: 19358756
    22. Both the location and orientation of CaM binding on the RyR2 are very similar to the skeletal muscle RyR1 isoform. PMID: 22067155
    23. PKC and CaM mRNA expression was downregulated in the hippocampus of baby rats with chronic lead exposure. PMID: 18761789
    24. molecular mechanisms of the phosphorylation-dependent regulation of NHE1 PMID: 21931166
    25. The present findings provide new insights on how MA interacts with CaM that may ultimately help in identification of the functional role of CaM-Gag interactions in the HIV replication cycle. PMID: 21799007
    26. Ca(2+) influx regulates assembly of a fully active CaN-calmodulin complex selectively on the tail of dynIxb and the complex is recruited to sites of activity-dependent bulk endocytosis in nerve terminals PMID: 21730063
    27. These results indicate that the aberrant formation of the activation link between CaMBD [(calmodulin)-binding domain] and CaMLD (CaM-like domain) of RyR is a key step in the development of hypertrophy in cultured cardiomyocytes. PMID: 21649588
    28. Calcium/calmodulin interferes with the association of AKAP150 with TRPV1. PMID: 21569553
    29. Data indicate that, in lactational rats, hippocampal neurogranin, CaMKII, calmodulin and calcineurin are involved in the brain impairment by developmental iodine deficiency and hypothyroidism. PMID: 20654708
    30. The BD-N and BD-C2 binding domains are sufficient for CaM binding to the native channel and BD-C1 is unable to bind CaM independently. PMID: 20523736
    31. translocation of CaM and CaMKII from the cytoplasm to the nucleus serves as messengers to transmit the pathogenic signal elicited in the surface membrane and in the RyR2 to the nuclear transcriptional sites to activate hypertrophy. PMID: 20433809
    32. CaM acts as a mediator in the Ca2+-dependent modulation of KCNQ channels. PMID: 12032157
    33. Calmodulin activity is critical for activation of volume-regulated anion channels in rat cerebral astrocytes. PMID: 15095369
    34. the majority of CaM nuclear entry occurs by facilitated mechanisms in all cell types examined, in part by a Ca2+-independent and in part by a Ca2+-dependent translocation mechanism PMID: 15522886
    35. the Ral-CaM complex defines a multifaceted regulatory mechanism for PLC-delta1 activation PMID: 15817490
    36. binding of 14-3-3, calmodulin and calcium channel beta-subunits to Kir/Gem is mutually exclusive PMID: 15860732
    37. These results explain how Calmodulin and iNOS coordinately function to form a stable complex that functions within the first 30 min following bacterial infection to upregulate the innate immune system involving macrophage activation. PMID: 16893173
    38. Ca2+-dependent CaM cascade might contribute to NMDA induced activation of PI-3K/Akt pathway. PMID: 17492691
    39. This study provides the first evidence that CaM and PKCdelta organize actin dynamics in the early endosomal compartment, thereby regulating the intracellular trafficking of EGFR. PMID: 17959830
    40. analysis of conformational changes of calmodulin upon Ca2+ binding PMID: 18178620
    41. The solution structures of complexes between calcium-saturated calmodulin (Ca (2+)/CaM) and a CaM-binding domain of the HIV-1 matrix protein p17 have been determined by small-angle X-ray scattering. PMID: 18553937
    42. Diabetes-induced acceleration of I(to) current inactivation is due to a reduced effect of CaMKII on I(to) channels as a result of a diabetes-induced reduction in calmodulin protein expression. PMID: 19088444
    43. In the intact SK channel complex, the N-lobe of calmodulin provides ligand-binding sites for channel gating, and that its ligand-binding properties are comparable to those of the N-lobe in isolated calmodulin. PMID: 19144926
    44. The oxidation-induced loss of secondary structure, as measured by circular dichroism, correlated with the rate of degradation for wild-type and mutant calmodulin containing Leu substitutions in the C-terminus. PMID: 19231837
    45. CaM bound to KCNQ2 acts as a Ca2+ sensor, conferring Ca2+ dependence to the trafficking of the channel to the plasma membrane and fully explaining the requirement of CaM binding for KCNQ2 function. PMID: 19494108

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  • 亞細胞定位:
    Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
  • 蛋白家族:
    Calmodulin family
  • 數據庫鏈接:

    KEGG: rno:24242

    UniGene: Rn.129719



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