Crystallin, beta B1 (CRYBB1) Kits ELISA

Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. De plus, nous expédions Crystallin, beta B1 Anticorps (29) et Crystallin, beta B1 Protéines (17) et beaucoup plus de produits pour cette protéine.

list all ELISA KIts Gène GeneID UniProt
CRYBB1 1414 P53674
CRYBB1 12960 Q9WVJ5
Anti-Rat CRYBB1 CRYBB1 25421 P02523
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Catalogue No. Reactivité Sensibilité Gamme Images Quantité Livraison Prix Détails
Souris 0.121 ng/mL 0.31 ng/mL - 20 ng/mL 96 Tests 13 to 16 Days
$757.89
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Humain < 0.188 ng/mL 0.313 ng/mL - 20 ng/mL   96 Tests 11 to 18 Days
$838.60
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Souris < 0.121 ng/mL 0.312 ng/mL - 20 ng/mL   96 Tests 11 to 18 Days
$902.56
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Plus Kits ELISA pour Crystallin, beta B1 partenaires d'interaction

Zebrafish Crystallin, beta B1 (CRYBB1) interaction partners

  1. fundamental transcriptional regulatory mechanism of the betaB1-crystallin gene has been well conserved between humans and zebrafish

Xenopus laevis Crystallin, beta B1 (CRYBB1) interaction partners

  1. The ontogeny and localization of the alphaA-crystallin and betaB1-crystallin during embryonic lens development and regeneration indicated a different development program, although they have identical origins, the ectoderm.

Human Crystallin, beta B1 (CRYBB1) interaction partners

  1. We examined a cohort of Chinese patients with congenital cataracts and studied the phenotypes and genotypes. Extralenticular abnormalities, such as microcornea and ocular coloboma, can also be found in patients with congenital cataracts. The phenotype of congenital cataracts associated with macular and optic disc coloboma was reported for the first time in this study.

  2. Our findings highlight the importance of the C-terminus in betaB1-crystallin in maintaining the crystalline function and stability, and provide a novel insight into the molecular mechanism underlying the pathogenesis of human autosomal dominant congenital cataract.

  3. CRYBB1 partial duplication ad complete duplication of CRYBA4 identified in a family with autosomal dominant congenital cataract.

  4. Molecular dynamic simulation studies indicated that the mutation decreased the subunit binding energy and modified the distribution of surface electrostatic potentials. More importantly, the mutation separated two interacting loops in the C-terminal domain, which shielded the hydrophobic core from solvent in native betaB1-crystallin.

  5. Congenital microcornea-cataract syndrome-causing mutation X253R increases betaB1-crystallin hydrophobicity to promote aggregate formation

  6. Despite the disruption of betaB1-crystallin assembly, the thermal stability of betaB1-crystallin was increased by the mutation accompanied by the reduction of thermal aggregation at high temperatures

  7. Sequencing of this gene revealed a homozygous c.171del mutation (p.N58Tfs*107) with a shared haplotype in all 16 children.

  8. study identified a novel heterozygous p.Ser129Arg mutation in CRYBB1 in a congenital cataract-microcornea syndrome family of Chinese origin

  9. The formation of beta-crystallin heteromers not only stabilizes the unstable acidic beta-crystallin but also protects them against aggregation during refolding from the stress-denatured states.

  10. The presence of significant amounts of small peptides derived from gammaS- and betaB1-crystallins in the water-insoluble fraction of the lens indicates that these interact tightly with cytoskeletal or membrane components.

  11. Analyses of 20 Chinese families with hereditary nuclear congenital cataract revealed 3 novel mutations. Two of these mutations (V146M and I21N) affected betaB2-crystallin (CRYBB2). One mutation (R233H) was detected in betaB1-crystallin (CRYBB1).

  12. Variant alleles of the CRYBB1 and CRYBB2 genes were found, none are considered pathogenic.

  13. Data show a significant demixing of gammaD and betaB1 i.e., large difference of composition in the two coexisting phases.

  14. Mutation G220X is associated with autosomal dominant cataract.

  15. 1.4 angstroms resolution crystal structure of a truncated version of human betaB1 that resembles an in vivo age-related truncation

  16. The molecular characterization of a UK family with an autosomal dominant congenital cataract associated with microcornea is reported

  17. fundamental transcriptional regulatory mechanism of the betaB1-crystallin gene has been well conserved between humans and zebrafish

  18. the sequence of betaB2-crystallin appears well optimized for domain swapping

  19. The dimeric intermediate may be a critical determinant for the life-long stability of the beta-crystallins and has important consequences on interactions with alpha-crystallin.

  20. The current study showed that a different mutation in the same gene causes an autosomal recessive form of the disease.

Mouse (Murine) Crystallin, beta B1 (CRYBB1) interaction partners

  1. The current study shows for the first time that two highly expressed lens crystallin genes, Cryba4 and Crybb1, can be simultaneously transcribed from adjacent bidirectional promoters and do not show nuclear accumulation.

  2. mixed betaB1- and betaA3-crystallins associate predominantly into heterotetramers in equilibrium with heterodimers

  3. Removal of the N-terminal extension of beta B1-crystallin has major effects on the physical properties of the protein by increasing the self-association potential and by blocking heteromolecular associations with beta A3-crystallin.

Pig (Porcine) Crystallin, beta B1 (CRYBB1) interaction partners

  1. Tissue expression analysis indicated that that swine SDHB, SNRPA and CRYBB1 genes were differentially expressed in tissues including fat, lung, muscle, small intestine, kidney, large intestine, spleen and liver.

Crystallin, beta B1 (CRYBB1) profil antigène

Antigen Summary

Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families\; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3.

Gene names and symbols associated with Crystallin, beta B1 (CRYBB1) Kits ELISA

  • crystallin, beta B1 (crybb1) anticorps
  • crystallin beta B1 S homeolog (crybb1.S) anticorps
  • crystallin beta B1 (CRYBB1) anticorps
  • crystallin beta B1 (crybb1) anticorps
  • crystallin beta B1 (Crybb1) anticorps
  • crystallin, beta B1 (Crybb1) anticorps
  • 3110006K12Rik anticorps
  • BB1CRY anticorps
  • CATCN3 anticorps
  • CRYB1 anticorps
  • CRYB11 anticorps
  • Crybb1 anticorps
  • CTRCT17 anticorps
  • zgc:92706 anticorps

Protein level used designations for Crystallin, beta B1 (CRYBB1) Kits ELISA

crystallin, beta B1 , crystallin B1 , beta B1 crystallin , betaB1-crystallin , beta-B1 crystallin , beta-crystallin B1 , eye lens structural protein , beta-35 , beta crystallin subunit beta B1

GENE ID SPECIES
114418 Danio rerio
397730 Xenopus laevis
458727 Pan troglodytes
486333 Canis lupus familiaris
550022 Xenopus (Silurana) tropicalis
100307054 Cavia porcellus
1414 Homo sapiens
12960 Mus musculus
25421 Rattus norvegicus
282205 Bos taurus
374000 Gallus gallus
780429 Sus scrofa
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