Crystallin, beta B2 Proteine (CRYbB2)

Crystallins are the dominant structural components of the vertebrate eye lens.. Zusätzlich bieten wir Ihnen CRYbB2 Antikörper (23) und CRYbB2 Kits (2) und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
CRYbB2 1415 P43320
CRYbB2 12961 P62696
CRYbB2 25422 P62697
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Top CRYbB2 Proteine auf antikoerper-online.de

Showing 10 out of 13 products:

Katalog Nr. Origin Quelle Konjugat Bilder Menge Anbieter Lieferzeit Preis Details
HOST_Wheat germ Human GST tag 10 μg Anmelden zum Anzeigen 7 bis 8 Tage
345,60 €
Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 26 bis 31 Tage
4.115,41 €
Details
HOST_Escherichia coli (E. coli) Maus His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Anmelden zum Anzeigen 26 bis 31 Tage
4.115,41 €
Details
HOST_HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Anmelden zum Anzeigen 6 bis 8 Tage
748,00 €
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Hefe Ratte His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.379,84 €
Details
Hefe Kaninchen His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.379,84 €
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Hefe Rind (Kuh) His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.379,84 €
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Hefe Hund His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.379,84 €
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Hefe Mesocricetus auratus His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.379,84 €
Details
Hefe Lithobates catesbeiana His tag   1 mg Anmelden zum Anzeigen 58 bis 70 Tage
2.379,84 €
Details

CRYbB2 Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human , ,
, ,
Mouse (Murine)

Rat (Rattus)

Am meisten referenzierte CRYbB2 Proteine

  1. Human CRYbB2 Protein expressed in Wheat germ - ABIN1350441 : Verma, Kumar, Babb, Timoney, Stevenson: Cross-reactivity of antibodies against leptospiral recurrent uveitis-associated proteins A and B (LruA and LruB) with eye proteins. in PLoS neglected tropical diseases 2010 (PubMed)

Weitere Proteine zu Crystallin, beta B2 (CRYbB2) Interaktionspartnern

Cow (Bovine) Crystallin, beta B2 (CRYbB2) Interaktionspartner

  1. Results show that both betaB2- and betaA3-crystallin (zeige CRYBA1 Proteine) 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 (zeige CRYAA Proteine), betaB2- and gammaS-(betaS)-crystallins.

Human Crystallin, beta B2 (CRYbB2) Interaktionspartner

  1. 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 (zeige CRYBB1 Proteine).

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

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

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

  5. 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.

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

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

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

  9. A novel missense mutation, p.Arg188His, in CRYBB2 is associated with congenital cataract in a family of Croatian origin.

  10. The Asp (zeige ASIP Proteine) residue at position 4 of betaB2-crystallin in the lenses of the aged human eye lenses undergoes a significant degree of inversion and isomerization to the biologically D-beta-Asp (zeige ASIP Proteine).

Mouse (Murine) Crystallin, beta B2 (CRYbB2) Interaktionspartner

  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 (zeige CAMK4 Proteine) 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 (zeige CRYBA1 Proteine).

  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 (zeige CRYAB Proteine) to betaB2- and gammaC-crystallin (zeige CRYGC Proteine).

  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.

CRYbB2 Protein Überblick

Protein Überblick

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

Genbezeichner und Symbole assoziert mit Crystallin, beta B2 Proteine (CRYbB2)

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

Bezeichner auf Proteinebene für Crystallin, beta B2 Proteine (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 SPEZIES
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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