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anti-Human CRY2 Antibodies:
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Human Polyclonal CRY2 Primary Antibody for IHC (p), ELISA - ABIN4369822
Allikmets, Gerrard, Hutchinson, Dean: Characterization of the human ABC superfamily: isolation and mapping of 21 new genes using the expressed sequence tags database. in Human molecular genetics 1997
Show all 3 Pubmed References
Human Polyclonal CRY2 Primary Antibody for IHC (p), WB - ABIN390080
Ozgur, Sancar: Purification and properties of human blue-light photoreceptor cryptochrome 2. in Biochemistry 2003
Show all 6 Pubmed References
Cow (Bovine) Polyclonal CRY2 Primary Antibody for IHC, WB - ABIN2784909
Currie, Doherty, Sillar: Deep-brain photoreception links luminance detection to motor output in Xenopus frog tadpoles. in Proceedings of the National Academy of Sciences of the United States of America 2016
Molecular basis for blue light-dependent phosphorylation of Arabidopsis CRY2 has been described.
The results demonstrate a CRY-BIC negative-feedback circuitry that regulates the activity of each other.
Verticillium dahliae PevD1 indirectly activates Arabidopsis CRY2 by antagonizing NRP functions. The promotion of CRY2-mediated flowering by a fungal effector outlines a novel pathway by which an external stimulus is recognized and transferred in changing a developmental program.
CRY2-CIB1 and CRY2-CRY2 interactions are governed by well-separated protein interfaces at the two termini of CRY2.
Exposure to blue light is required for an in vivo-association of CRY1 and CRY2 with COP1.
Data show that the effect of 3-bromo-7-nitroindazole (3B7N) treatment on gene expression in cryptochromes cry1cry2 is considerably smaller than that in the wild type, indicating that 3B7N specifically interrupts cryptochrome function in the control of seedling development in a light-dependent manner.
It describes minimal functional CRY2 and CIB1 domains maintaining light-dependent interaction and new signaling mutations affecting Arabidopsis thaliana cryptochrome 2 (AtCRY2) photocycle kinetics.
this study identified BIC1 (blue-light inhibitor of cryptochromes 1) as an inhibitor of plant cryptochromes that binds to CRY2 to suppress the blue light-dependent dimerization, photobody formation, phosphorylation, degradation, and physiological activities of CRY2.
the blue light-dependent CRY2 degradation is significantly impaired in the temperature-sensitive cul1 mutant allele (axr6-3), especially under the non-permissive temperature.
For growth under a canopy, where blue light is diminished, CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5.
Arabidopsis thaliana cry2 proteins containing Trp triad mutations indeed undergo robust photoreduction in living cultured insect cells.
data showed that mutations in the serine residues within and outside the serine cluster diminished blue light-dependent CRY2 phosphorylation, degradation, and physiological activities.
Our study demonstrates that CIBs function redundantly in regulating CRY2-dependent flowering, and that different CIBs form heterodimers to interact with the non-canonical E-box DNA in vivo.
Studies show that CK1.3 (At4g28880) and CK1.4 (At4g28860) directly phosphorylate CRY2 at Ser-587 and Thr-603 in vitro and negatively regulate CRY2 stability, which are stimulated by blue light.
Based on the loss of degradation of cry2 after prolonged darkness and loss of reversibility of photoactivated cry1 by a pulse of green light, we estimate the in vivo half-lives of the signaling states of cry1 and cry2 to be in the range of 5 and 16 min.
Data indicate that although cryptochrome 2 physically interacts with CIB1 in response to blue light, ZEITLUPE and LOV KELCH PROTEIN 2 are required for the function and blue-light suppression of degradation of CIB1.
fusing AtCRY2 to the TopBP1 DNA damage checkpoint protein, light-induced AtCRY2 PBs can be used to activate DNA damage signaling pathway in the absence of DNA damage
Data indicate that the green light (GL) opposition of red light (RL) responses persists in phyA, phyB, cry1cry2 and phot2 mutants, and the response requires phot1 and NPH3.
Degradation of Arabidopsis CRY2 is regulated by SPA1, Spa2, Spa4 proteins and phytochrome A.
The photoexcited cryptochromes form oligomers, preceding other biochemical changes of CRY2, facilitate photobody formation, signal amplification, and propagation, as well as desensitization by degradation.
CRY2 levels (ng/mL) were markedly higher in both Metabolic syndrome (MetS) groups (non-diabetic and pre-diabetic/diabetic) (all with p-value < 0.001). A reciprocal melatonin-CRY2 relationship was observed in the MetS (non-diabetic) group (p-value = 0.003).
Independent silencing of CRY1 and CRY2 genes in HAC15 cells resulted in a mild upregulation of HSD3B2 without affecting HSD3B1 expression. In conclusion, our results support the hypothesis that CRY1 and CRY2, being AngII-regulated genes, and showing a differential expression in APAs when compared with the adjacent adrenal cortex, might be involved in adrenal cell function, and in the regulation of aldosterone production
CRY2 may be an anti-oncogene in osteosarcoma.
CRY1/2 serve as corepressors for many NRs.
data indicate an oncogenic role of miR-181d in CRC by promoting glycolysis, and miR-181d/CRY2/FBXL3/c-myc feedback loop might be a therapeutic target for patients with CRC.
In the longitudinal analysis, CRY2 SNP rs61884508 was protective from worsening of problematicity of seasonal variations of mood disorder. In the cross-sectional analysis, CRY2 SNP rs72902437 showed evidence of association with problematicity of seasonal variations, as did SNP rs1554338 (in the MAPK8IP1 and downstream of CRY2).
The earlier reported association of CRY2 variants with dysthymia was confirmed and extended to major depressive disorder.
These results demonstrate that CRY2 stability controlled by FBXL3 plays a key role in the regulation of human sleep wake behavior.
The FOXM1 is a negative regulator of CRY2 in breast cancer via enhancing methylation in CRY2 promoter and its high expression is an independent predictor of favorable MR-free survival in ER+ breast cancer patients.
CRY2 and FBXL3 cooperatively degrade c-MYC preventing the development of cancer.
The present study identified USP7 and TDP-43 as the regulators of CRY1 and CRY2, underscoring the significance of the stability control process of CRY proteins for period determination in the mammalian circadian clockwork.
For the first time, we show that Cry 2 rs2292910 and MTNR1B rs3781638 are associated with osteoporosis in a Chinese geriatric cohort.
Altered CRY1 and CRY2 expression patterns and the interplay with the genetic landscape in colon cancer cells may underlie phenotypic divergence.
Given the distinct characteristics of the C-terminal tails of the CRY1 and CRY2 proteins, our study addresses a long-standing hypothesis that the ratio of these two CRY molecules affects the clock period.
data may point to CRY2 as a novel switch in hepatic fuel metabolism promoting triglyceride storage and, concomitantly, limiting glucose production
Data indicate that cryptochrome 2 (CRY2) knockdown leads to chemosensitivity of colorectal cancer cell lines.
CRY2 and REV-ERB ALPHA as the clock genes upregulated in obesity during the 24 h period and that REV-ERB ALPHA is an important gene associated with MS.
these observations suggest a biologically plausible season-dependent association between SNPs at CRY1, CRY2 and MTNR1B and glucose homeostasis.
CRY1 and CRY2 variants showed nominal association with the metabolic syndrome components, hypertension and triglyceride levels.
These findings suggest that the core circadian gene CRY2 is associated with breast cancer progression and prognosis, and that knockdown of CRY2 causes the epigenetic dysregulation of genes involved in cancer-relevant pathways
Circadian clock cryptochrome proteins Cry1 and Cry2 regulate autoimmunity.
CRY1/2 seem to repress a distinct subset of PPAR delta target genes in muscle compared to the co-repressor NCOR1. In vivo, genetic disruption of Cry1 and Cry2 enhances sprint exercise performance in mice.
In vivo knockdown of Rfk, Riboflavin (vitamin B2) kinase essential for FAD synthesis, altered the expression rhythms of CRY1, CRY2, and PER1
Data show that cryptochrome Cry1 and Cry2 expression must be circadian and appropriately phased to support rhythms, and arginine vasopressin (AVP) receptor signaling is required to impose circuit-level circadian function.
Data suggest that cryptochromes (Cry1 and Cry2) mediate periodic binding of Ck2b (casein kinase 2beta) to Bmal1 (aryl hydrocarbon receptor nuclear translocator-like protein) and thus inhibit Bmal1-Ser90 phosphorylation by Ck2a (casein kinase 2alpha).
Cry2 exerts a critical role in the control of depression-related emotional states and modulates the chronobiological gene expression profile in the mouse amygdala.
Cry1/Cry2-deficient mice had significantly lower N6- methyladenosine methylation of RNA and lost the circadian rhythm of N6-methyladenosine levels in RNA.
Data show that the intermolecular zinc finger is important for period circadian protein (PER2)-cryptochrome 2 (CRY2) complex formation.
Report compression of daily activity time in Cry2 mutant mice.
Data show that Ser557 phosphorylation of CRY2 promotes CRY2 degradation and inhibits the overaccumulation of the CRY2-PER2 complex in the nucleus.
the daily dissonance between peripheral clocks and the environment did not affect the lifespan of Cry1(-/-) or Cry2(-/-) mice.
Demonstrate opposing actions for Cry2 and Per1 on Per1 target genes, supporting the potential Cry2-Clock/Bmal1-dependent mechanism underlying Per1 action in the liver and kidney.
Cry2 knockout mice are susceptible to diet-induced obesity.
In both CRY2 and CRY1-deficient backgrounds, circadian rhythms of wheel-running and suprachiasmatic nucleus show increased period length.
the levels of CAVIN-3 inversely correlated with those of PER2 and CRY2, and CAVIN-3 might thus regulate both the abundance and the stability of PER:CRY complexes
In the suprachiasmatic nucleus, uncoupled Cry1-/- cells are nearly arrhythmic, whereas Cry2-/- cells are strongly rhythmic with long period.
crystal structures of mammalian CRY2 in its apo, FAD-bound and FBXL3-SKP1-complexed forms
FBXL21 plays a dual role: protecting CRY 1/2 proteins (CRY) from FBXL3 degradation in the nucleus and promoting CRY degradation within the cytoplasm.
member of a family of blue-light photoreceptors\; may regulate circadian rhythm
, cryptochrome 2
, cryptochrome Cry2
, cryptochrome 2 (photolyase-like)
, growth-inhibiting protein 37