anti-Crystallin, beta B2 (CRYbB2) Antibodies

Crystallins are the dominant structural components of the vertebrate eye lens.. Additionally we are shipping CRYbB2 Proteins (13) and CRYbB2 Kits (2) and many more products for this protein.

list all antibodies Gene Name GeneID UniProt
CRYbB2 1415 P43320
CRYbB2 12961 P62696
CRYbB2 25422 P62697
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Top anti-CRYbB2 Antibodies at

Showing 10 out of 23 products:

Catalog No. Reactivity Host Conjugate Application Images Quantity Supplier Delivery Price Details
Human Mouse Un-conjugated IHC, WB 100 μL Log in to see 16 Days
Mouse Rabbit Un-conjugated ICC, IHC, IP, WB 100 μg Log in to see 15 to 18 Days
Human Mouse Un-conjugated ELISA, WB Detection limit for recombinant GST tagged CRYBB2 is 3 ng/ml as a capture antibody. Western Blot analysis of CRYBB2 expression in transfected 293T cell line by CRYBB2 monoclonal antibody (M02), clone 1F1.Lane 1: CRYBB2 transfected lysate (Predicted MW: 23.4 KDa).Lane 2: Non-transfected lysate. 100 μg Log in to see 11 to 12 Days
Human Rabbit Un-conjugated IHC, IHC (p) Immunohistochemistry-Paraffin: CRYBB2 Antibody [NBP2-13876] Staining of human kidney shows moderate cytoplasmic positivity in fraction of tubules. 0.1 mL Log in to see 10 to 13 Days
Human Mouse Un-conjugated ELISA, WB   100 μg Log in to see 7 to 9 Days
Mouse Rabbit Biotin ELISA, WB   100 μg Log in to see 7 to 9 Days
Mouse Rabbit FITC ELISA, WB   100 μg Log in to see 7 to 9 Days
Human Rabbit Un-conjugated IHC, WB   50 μL Log in to see 7 to 9 Days
Mouse Rabbit Un-conjugated ELISA, WB   100 μg Log in to see 7 to 9 Days
Rat Mouse Biotin ELISA, WB   200 μg Log in to see 7 to 9 Days

CRYbB2 Antibodies by Reactivity, Application, Clonality and Conjugate

Attributes Applications Host Clonality Conjugate
Human ,
Mouse (Murine)
Rat (Rattus)

More Antibodies against CRYbB2 Interaction Partners

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

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

Human Crystallin, beta B2 (CRYbB2) interaction partners

  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 (show CRYBB1 Antibodies).

  2. This is the first study to analyze the association between genetic variations in the CRYBB2 gene with PCa (show FLVCR1 Antibodies). 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 (show ASIP Antibodies) 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 Antibodies).

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 (show CAMK4 Antibodies) 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 (show CRYBA1 Antibodies).

  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 (show MIP Antibodies) and all crystallins, with the extent of interactions decreasing from alphaA- and alphaB-crystallin (show CRYAB Antibodies) to betaB2- and gammaC-crystallin (show CRYGC Antibodies).

  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 Antigen Profile

Protein Summary

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

Gene names and symbols associated with CRYbB2

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

Protein level used designations for 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

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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