KRIT1 Antibody, FITC conjugated

Code CSB-PA012501LC01HU
Size US$166
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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) KRIT1 Polyclonal antibody
Uniprot No.
Target Names
KRIT1
Alternative Names
Ankyrin repeat containing protein Krit1 antibody; CAM antibody; CCM 1 antibody; CCM1 antibody; Cerebral cavernous malformations 1 antibody; Cerebral cavernous malformations 1 protein antibody; Krev interaction trapped 1 antibody; Krev interaction trapped protein 1 antibody; KRIT 1 antibody; KRIT1 ankyrin repeat containing antibody; KRIT1 antibody; KRIT1_HUMAN antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Krev interaction trapped protein 1 protein (471-585AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
FITC
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
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.

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Target Background

Function
Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-dependent and independent manner, and inhibits ERK1/2 phosphorylation indirectly through activation of the DELTA-NOTCH cascade. Acts in concert with CDH5 to establish and maintain correct endothelial cell polarity and vascular lumen and these effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction, and cell junction stabilization. Plays a role in integrin signaling via its interaction with ITGB1BP1; this prevents the interaction between ITGB1 and ITGB1BP1. Microtubule-associated protein that binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes in a GTP-bound RAP1-dependent manner. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Regulates the homeostasis of intracellular ROS through an antioxidant pathway involving FOXO1 and SOD2. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS through the modulation of FOXO1 and SOD2 levels.
Gene References into Functions
  1. We report a case of a highly penetrant but variably expressed form of cerebral cavernous malformation syndrome with cerebral, cutaneous, and retinal cavernomas in a family found to harbor a nonsense mutation of the CCM1 gene. PMID: 28867399
  2. Case-control study to investigate the possible association of others polymorphisms (c.485+65 C/G, c.989+63 C/G, c.1980 A/G in CCM1 gene, c.472+127 C/T in CCM2 and c.150 G/A in CCM3) with cerebral cavernous malformations. The five polymorphisms were characterized in 64 sporadic patients and in 90 healthy controls by ASO-PCR. Results suggest that some polymorphisms in CCM genes could play an important role in the disease. PMID: 28870584
  3. The finding of this study suggests that the novel nonsense mutation c.1159G>T in CCM1 gene is associated with multiple cerebral cavernous malformations, and that CCM1 haploinsufficiency may be the underlying mechanism of multiple cerebral cavernous malformations. PMID: 26643368
  4. Adrenal calcifications identified on CT scans are common in patients with fCCM and may be a clinically silent manifestation of disease. PMID: 28318403
  5. A novel KRIT1 heterozygous nonsense mutation (c.1864C>T) segregated with familial cerebral cavernous malformation in a Chinese family. PMID: 28255959
  6. A novel heterozygous insertion KRIT1 mutation identified in cerebral cavernous malformation patient. mRNA level of KRIT1 were significantly decreased in FCCM subjects. PMID: 28160210
  7. A novel nonsense mutation in CCM1 were detected in cerebral cavernous malformations patient. PMID: 28000143
  8. nuclear-cytoplasmic shuttling of ICAP1 influences both integrin activation and KRIT1 localization, presumably impacting nuclear functions of KRIT1. PMID: 28003363
  9. New Krit1 mutations segregated with cerebral cavernous malformation in Chinese families. PMID: 27649701
  10. Studies suggest that the 3 proteins of the Cerebral Cavernous Malformations (CCM) complex KRIT1/CCM1, CCM2/malcavernin and CCM3/PDCD10 not only require one another for reciprocal stabilization, but also act as a platform for signal transduction. PMID: 26356566
  11. Valproic acid reduces intracellular ROS level by the modulation of KRIT1 and its correlated proteins, FoxO1, SOD2, and cyclin D1 in mesenchymal stromal cells. PMID: 25203678
  12. KRIT1 protects endothelial integrity during mechanical stress and trap6 exposure. PMID: 25923142
  13. Novel CCM1 deletion mutation segregated with cerebral cavernous angioma in a Chinese family. PMID: 25185960
  14. Case Report: cerebral cavernous malformations and unilateral moyamoya disease in a patient with a new mutation in the KRIT-1 /CCM1 gene. PMID: 25413039
  15. Here we discuss nuclear functions of adhesion complex proteins with a special focus on the CCM-1/KRIT-1 protein, which may turn out to be yet another adhesion complex protein with a second life. PMID: 24714220
  16. Data find that several disease-associated missense mutations in CCM2 have the potential to interrupt the KRIT1-CCM2 interaction by destabilizing the CCM2 PTB domain and that a KRIT1 mutation also disrupts this interaction PMID: 25525273
  17. Genetic analysis of familial cerebral cavernous malformation in Japanese involved the KRIT1 gene. PMID: 25707093
  18. Data indicate the regulatioin of vascular endothelial growth factor (VEGF) signaling in Krev-interaction trapped 1 (KRIT1)-depleted endothelial cells. PMID: 25320085
  19. Data indicate that the major binding site for binding of sorting nexin 17 (SNX17) is confined to the NPXF2 motif in cytoplasmic adaptor protein Krev interaction trapped 1 (KRIT1). PMID: 25059659
  20. Our findings demonstrate that CCM1 c.263-10A > G mutation is associated with cerebral cavernous malformations. PMID: 25086949
  21. Prevalence, frequency and characterization of CCM1, CCM2 and CCM3 variants in cerebral cavernous malformation Spanish patients. PMID: 24466005
  22. These preliminary data indicate a still undescribed and unknown role for KRIT1 inside the nucleus. PMID: 24705002
  23. with the reported role of c-Jun in vascular dysfunctions triggered by oxidative stress, our findings shed new light on the molecular mechanisms underlying KRIT1 function and CCM pathogenesis. PMID: 24291398
  24. DNA sequencing and deletion/duplication testing of the CCM1, CCM2, and CCM3 genes in the proband revealed a CCM1 c.601CNG mutation. PMID: 24007869
  25. The identification of other four new mutations in 40 sporadic patients with either single or multiple cerebral cavernous malformations, is reported. PMID: 24058906
  26. A high resolution crystal structure and minimal binding region with integrin cytoplasmic domain-associated protein-1 (ICAP1) has been determined for KRIT1. PMID: 23695561
  27. KRIT1 mutations are associated with cerebral cavernous malformation in some Japanese patients. PMID: 23485406
  28. we present a rare and interesting case of monozygotic twins heterozygous for the CCM1 germline mutation and discuss their similar age and type of disease manifestation and their beginning divergent clinical course PMID: 23584803
  29. These data show that HEG1 can recruit the Rap1-KRIT complex to the plasma membrane. PMID: 23814056
  30. Our findings suggest that miR-21 promotes tumor cell growth, at least in part, by down-modulating the potential tumor suppressor KRIT1. PMID: 23872064
  31. Genetic testing identified a truncating mutation in the KRIT1 gene in one individual and confirmed the diagnosis of familial cerebral cavernomas as the cause of epilepsy in a family. PMID: 22699465
  32. The structural basis for KRIT1 antagonized ICAP1-modulated integrin-beta1 activation. PMID: 23317506
  33. Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1) PMID: 22577140
  34. These studies establish that the direct physical interaction of Rap1 with KRIT1 enables the translocation of microtubule-sequestered KRIT1 to junctions, thereby supporting junctional integrity and cardiovascular development PMID: 21633110
  35. Among familial cases of Cerebral cavernous malformations 67% had a mutation in CCM1, 5.5% in CCM2, and 5.5% in CCM3 PMID: 21029238
  36. Genetic variations could interfere with the proper CCM1/CCM2/CCM3 protein complex, thus explaining the observed clinical variability in cerebral cavernous malformations in a large family. PMID: 20419355
  37. Here we report a novel deletion of CCM1 that correlates strongly with cerebral cavernous malformations in a Chinese family. We predict this deletion produces a premature stop code (TGA) at NT 1228, resulting in a truncated protein of 409 amino acids. PMID: 20884211
  38. We described the complete loss of 7q21.2 locus encompassing the KRIT1 gene and 4 flanking genes in a CCM family by using a dense set of 12 microsatellite markers. PMID: 20798775
  39. Frame shift mutation in KRIT1 gene is associated with cerebral and multiple spinal cavernous malformations. PMID: 20689144
  40. We have identified a novel mutation in the KRIT1/CCM1 gene in a patient with both CCM and retinal cavernous hemangioma. PMID: 20306072
  41. The KRIT1-CCM2 interaction regulates endothelial junctional stability and vascular barrier function by suppressing activation of the RhoA/ROCK signaling pathway. This pathway is dysregulated in human cerebral cavernous malformation endothelium. PMID: 20308363
  42. Familial CCM1 cavernous malformations are unlikely to be associated with developmental venous anomalies, and sporadic malformations have a high rate of association with them PMID: 19833796
  43. KRIT1/CCM1 mutation in a patient with retinal and cerebral cavernous angiomas. PMID: 11831930
  44. Integrin-binding protein also interacts with Krit 1 protein, cause of CCM1. (ICAP-1, integrin cytoplasmic domain-associated protein 1) PMID: 11854171
  45. In familial CCM1 samples, two new Krit1 mutations have been reported in four new upstream exons and six additional mutations have been discovered in the previously identified exons, demonstrating a mutation frequency of 47% in the 27 families studied. PMID: 11914398
  46. RNA analysis reveals that two point mutations actually activate cryptic splice-donor sites, causing aberrant splicing and leading to a frameshift and protein truncation PMID: 11941540
  47. Krit1 mRNA expression in adult tissues PMID: 12204286
  48. Mutations in Krit1 are associated with familial cerebral cavernous malformations, but seldom a cause of sporadic cavernomas PMID: 12682320
  49. Identification of a novel KRIT1 mutation in an Italian family with cerebral cavernous malformation by the protein truncation test. PMID: 12810002
  50. We report a mutation causing a premature termination triplet in exon 17 of the Krit1 gene in a family with diagnoses of cerebral cavernous angioma PMID: 12877753

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Involvement in disease
Cerebral cavernous malformations 1 (CCM1)
Subcellular Location
Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell junction. Note=KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Association with RAP1 relocalizes KRIT1 from microtubules to cell junction membranes. Translocates from the cytoplasm along microtubules to the cell membrane in a ITGB1BP1-dependent manner.
Tissue Specificity
Low levels in brain. Very weak expression found in heart and muscle.
Database Links

HGNC: 1573

OMIM: 116860

KEGG: hsa:889

STRING: 9606.ENSP00000344668

UniGene: Hs.531987

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