Rat calmodulin,CAM ELISA Kit

Code CSB-E09753r
Size 96T,5×96T,10×96T
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Product Details

Target Name
calmodulin 1 (phosphorylase kinase, delta)
Alternative Names
Calm1 ELISA kit; Calm ELISA kit; Cam ELISA kit; Cam1 ELISA kit; CaMICalmodulin-1 ELISA kit
Abbreviation
CALM1
Uniprot No.
Species
Rattus norvegicus (Rat)
Sample Types
serum, plasma
Detection Range
15.6 ng/mL-1000 ng/mL
Sensitivity
3.9 ng/mL
Assay Time
1-5h
Sample Volume
50-100ul
Detection Wavelength
450 nm
Research Area
Signal Transduction
Assay Principle
quantitative
Measurement
Sandwich
Precision
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.
Linearity
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
Recovery
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
Typical Data
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
Troubleshooting
and FAQs
Storage
Store at 2-8°C. Please refer to protocol.
Lead Time
3-5 working days after you place the order, and it takes another 3-5 days for delivery via DHL or FedEx
Description

This Rat CALM1 ELISA Kit was designed for the quantitative measurement of Rat CALM1 protein in serum, plasma. It is a Sandwich ELISA kit, its detection range is 15.6 ng/mL-1000 ng/mL and the sensitivity is 3.9 ng/mL.

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Target Background

Function
(From Uniprot)
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.
Gene References into Functions
  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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Subcellular Location
Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families
Calmodulin family
Database Links

KEGG: rno:24242

UniGene: Rn.129719

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