Crystallin, beta B2 Protéines (CRYbB2)

Crystallins are the dominant structural components of the vertebrate eye lens.. De plus, nous expédions CRYbB2 Anticorps (31) et CRYbB2 Kits (8) et beaucoup plus de produits pour cette protéine.

afficher tous les protéines Gène GeneID UniProt
CRYbB2 1415 P43320
CRYbB2 12961 P62696
CRYbB2 25422 P62697
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Top CRYbB2 Protéines sur anticorps-enligne.fr

Showing 10 out of 15 products:

Catalogue No. Origin Source Conjugué Images Quantité Fournisseur Livraison Prix Détails
Escherichia coli (E. coli) Humain His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Connectez-vous pour afficher 30 to 35 Days
$5,465.26
Détails
Escherichia coli (E. coli) Souris His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Connectez-vous pour afficher 30 to 35 Days
$5,465.26
Détails
Wheat germ Humain GST tag 10 μg Connectez-vous pour afficher 11 to 12 Days
$414.29
Détails
HEK-293 Cells Humain Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Connectez-vous pour afficher Disponible
$814.00
Détails
Escherichia coli (E. coli) Souris His tag   100 μg Connectez-vous pour afficher 15 to 18 Days
$560.00
Détails
Levure Rat His tag   1 mg Connectez-vous pour afficher 60 to 71 Days
$2,498.83
Détails
Levure Lapin His tag   1 mg Connectez-vous pour afficher 60 to 71 Days
$2,498.83
Détails
Levure Hamsters dorés syriens His tag   1 mg Connectez-vous pour afficher 60 to 71 Days
$2,498.83
Détails
Levure Chien His tag   1 mg Connectez-vous pour afficher 60 to 71 Days
$2,498.83
Détails
Levure Boeuf (Vache) His tag   1 mg Connectez-vous pour afficher 60 to 71 Days
$2,498.83
Détails

CRYbB2 Protéines protéines par origine et source

Origin Exprimée danse Conjugué
Human , ,
, ,
Mouse (Murine)

Rat (Rattus) ,

Plus protéines pour Crystallin, beta B2 (CRYbB2) partenaires d'interaction

Cow (Bovine) Crystallin, beta B2 (CRYbB2) interaction partners

  1. Results show that both betaB2- and betaA3-crystallin (Montrer CRYBA1 Protéines) bind calcium with moderate affinity.

  2. combined with previously reported observations of alpha-crystallin quaternary structure have led us to propose a structural model of how activated alpha-crystallin chaperones unfolded betaB2-crystallin

  3. Mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin (Montrer CRYAA Protéines), betaB2- and gammaS-(betaS)-crystallins.

Human Crystallin, beta B2 (CRYbB2) interaction partners

  1. conserved Trp (Montrer TBPL1 Protéines) residues might play a more crucial role in the correct folding and structural integrity of beta-crystallin domains than in gamma-crystallins

  2. The first pregnancy was terminated in week 22. Copy number variation analysis revealed, in both the aborted fetus and the mother, a 495 kb duplication at 22q11.23 encompassing CRYBB3 (Montrer CRYbB3 Protéines) and CRYBB2

  3. Study demonstrates that, in solution, human betaB2-crystallin is not domain swapped and exhibits a face-en-face dimer structure similar to the crystal structure of truncated betaB1-crystallin (Montrer CRYBB1 Protéines).

  4. This is the first study to analyze the association between genetic variations in the CRYBB2 gene with PCa (Montrer FLVCR1 Protéines). rs9608380, associated with Prostate cancer, is a potentially functional variant

  5. Congenital cataracts were caused by the de novo gene conversion event in CRYBB2 in a consanguineous Jewish Ashkenazi family.

  6. missense mutation in CRYBB2 gene leads to progressive congenital membranous cataract by impacting the solubility and function of betaB2-crystallin

  7. The distinct behaviors of the mutants suggested that the residue at position 188 might play a regulatory role in betaB2-crystallin aggregation/fibrillization but not reside in the core of the aggregates/fibrils.

  8. The last strand at the C-terminus of CRYBB2 is important for the protein stability and assembly.

  9. Identification of the first CRYBB2 mutation in an Italian family causing a clinical picture of autosomal dominant congenital cataract.

  10. The congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of betaB2-crystallin.

Mouse (Murine) Crystallin, beta B2 (CRYbB2) interaction partners

  1. In conclusion, CRYBB2 regulates expression of different lncRNAs to influence ovary development

  2. ovaries from female Crybb2(-/-) mice exhibited significantly reduced numbers of primordial, secondary and pre-ovulatory follicles when compared with WT mice, while the rate of atretic follicles was also increased

  3. BetaB2-crystallin has a role in hippocampal function and behavioral phenotypes.

  4. The reduced fertility of Crybb2 knockout male mice may result from the disordered proliferation and apoptosis of germ cells in the testis, possibly due to reduced CaMKIV (Montrer CAMK4 Protéines) from the loss of Crybb2.

  5. Removal of both amino- and carboxyl-terminal extensions of recombinant crystallin beta B2 increases the entropy and enthalpy of dimer binding but to a lesser degree than occurs in truncated recombinant beta A3 crystallin (Montrer CRYBA1 Protéines).

  6. Thus, some of the fiber differentiation processes are likely mediated by RTK-dependent but Ras-independent pathways.

  7. betaB2-crystallin is expressed in developing and mature sperm and mice of both sexes harboring the Philly mutation in the betaB2-crystallin gene are subfertile when analyzed on a Swiss Webster genetic background.

  8. presence of measurable interactions between MIP26 and all crystallins, with the extent of interactions decreasing from alphaA- and alphaB-crystallin (Montrer CRYAB Protéines) to betaB2- and gammaC-crystallin (Montrer CRYGC Protéines).

  9. These results confirm the third allele of Crybb2 in the mouse that also affected exon 6 and the fourth Greek key motif. Moreover, expression analysis of Crybb2 identified for the first time distinct regions of expression in the brain.

  10. BetaB2-crystallin is not essential for the normal development of a transparent lens in the mouse. It plays an increasingly important role in maintaining the transparency of the lens after birth.

Profil protéine CRYbB2

Profil protéine

Crystallins are the dominant structural components of the vertebrate eye lens.

Gene names and symbols associated with Crystallin, beta B2 Protéines (CRYbB2)

  • crystallin beta B2 S homeolog (crybb2.S)
  • crystallin, beta B2 (crybb2)
  • crystallin beta B2 (CRYBB2)
  • crystallin beta B2 (Crybb2)
  • crystallin, beta B2 (Crybb2)
  • crystallin, beta B2 (CRYBB2)
  • Aey2 Protéine
  • CCA2 Protéine
  • Cryb-2 Protéine
  • CRYB2 Protéine
  • CRYB2A Protéine
  • CTRCT3 Protéine
  • D22S665 Protéine
  • HaCryBB2 Protéine
  • MGC84803 Protéine
  • Phil Protéine

Protein level used designations for Crystallin, beta B2 Protéines (CRYbB2)

crystallin, beta B2 , beta-crystallin B2 , beta B2-crystallin , beta-B2 crystallin , beta-crystallin Bp , eye lens structural protein , Philly cataract , betaB2-crystallin , R.norvegicus CRYBB2 gene (crystallin, beta B2) , Beta-B2 crystallin , Beta-crystallin Bp , beta-B2-crystallin

GENE ID SPECIES
446980 Xenopus laevis
553182 Danio rerio
100144420 Macaca mulatta
100306964 Cavia porcellus
287011 Bos taurus
1415 Homo sapiens
12961 Mus musculus
25422 Rattus norvegicus
396088 Gallus gallus
486326 Canis lupus familiaris
100037715 Oryctolagus cuniculus
101842717 Mesocricetus auratus
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