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Crystallin, beta B2 Proteins (CRYbB2)

Crystallins are the dominant structural components of the vertebrate eye lens.. Additionally we are shipping CRYbB2 Antibodies (22) and CRYbB2 Kits (6) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
CRYbB2 1415 P43320
CRYbB2 12961 P62696
CRYbB2 25422 P62697
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Top CRYbB2 Proteins at antibodies-online.com

Showing 10 out of 13 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Wheat germ Human GST tag 10 μg Log in to see 9 Days
$405.71
Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
Yeast Cow His tag   1 mg Log in to see 56 to 66 Days
$2,498.83
Details
Yeast Mesocricetus auratus His tag   1 mg Log in to see 56 to 66 Days
$2,498.83
Details
Yeast Lithobates catesbeiana His tag   1 mg Log in to see 56 to 66 Days
$2,498.83
Details
Yeast Rabbit His tag   1 mg Log in to see 56 to 66 Days
$2,498.83
Details
Yeast Rat His tag   1 mg Log in to see 56 to 66 Days
$2,498.83
Details
Yeast Dog His tag   1 mg Log in to see 56 to 66 Days
$2,498.83
Details
Yeast Chicken His tag   1 mg Log in to see 56 to 66 Days
$2,541.00
Details

CRYbB2 Proteins by Origin and Source

Origin Expressed in Conjugate
Human , ,
,
Mouse (Murine)

Rat (Rattus)

Top referenced CRYbB2 Proteins

  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)

More Proteins for Crystallin, beta B2 (CRYbB2) Interaction Partners

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

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

Human Crystallin, beta B2 (CRYbB2) interaction partners

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

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

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

  4. 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.

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

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

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

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

  9. The Asp (show ASIP Proteins) 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 (show ASIP Proteins).

  10. analysis of a novel CRYBB2 gene mutation, resulting in the amino substitution p. A2V in a Chinese family with posterior subcapsular congenital cataracts

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

  1. 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

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

  3. 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 (show CAMK4 Proteins) from the loss of Crybb2.

  4. 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 (show CRYBA1 Proteins).

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

  6. 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.

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

  8. 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.

  9. 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 Profile

Protein Summary

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

Gene names and symbols associated with Crystallin, beta B2 Proteins (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

Protein level used designations for Crystallin, beta B2 Proteins (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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