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Crystallin, beta B1 Proteins (CRYBB1)

Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Additionally we are shipping Crystallin, beta B1 Antibodies (25) and Crystallin, beta B1 Kits (6) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
CRYBB1 1414 P53674
CRYBB1 12960 Q9WVJ5
CRYBB1 25421 P02523
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Top Crystallin, beta B1 Proteins at antibodies-online.com

Showing 10 out of 19 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price 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
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) Human His tag 100 μg Log in to see 7 to 8 Days
$286.00
Details
HOST_Wheat germ Human GST tag 10 μg Log in to see 9 Days
$405.71
Details
Yeast Chicken His tag   1 mg Log in to see 56 to 66 Days
$2,603.33
Details
Yeast Wild boar His tag   1 mg Log in to see 56 to 66 Days
$2,634.50
Details
Yeast Rat His tag   1 mg Log in to see 56 to 66 Days
$2,638.17
Details
Yeast Cow His tag   1 mg Log in to see 56 to 66 Days
$2,647.33
Details
HOST_Escherichia coli (E. coli) Rat His tag   100 μg Log in to see 11 to 13 Days
$598.40
Details
HOST_Escherichia coli (E. coli) Human His tag   1 mg Log in to see 3 to 4 Days
$2,524.50
Details

CRYBB1 Proteins by Origin and Source

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

Rat (Rattus) ,

Top referenced Crystallin, beta B1 Proteins

  1. Human CRYBB1 Protein expressed in Escherichia coli (E. coli) - ABIN667015 : Annunziata, Pande, Pande, Ogun, Lubsen, Benedek: Oligomerization and phase transitions in aqueous solutions of native and truncated human beta B1-crystallin. in Biochemistry 2005 (PubMed)
    Show all 2 references for ABIN667015

More Proteins for Crystallin, beta B1 (CRYBB1) Interaction Partners

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 (show CRYAA Proteins) 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. 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

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

  3. 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 (show CRYbB2 Proteins)). One mutation (R233H) was detected in betaB1-crystallin (CRYBB1).

  4. Variant alleles of the CRYBB1 and CRYBB2 (show CRYbB2 Proteins) genes were found, none are considered pathogenic.

  5. Mutation G220X is associated with autosomal dominant cataract.

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

  7. the sequence of betaB2-crystallin (show CRYbB2 Proteins) appears well optimized for domain swapping

  8. study identified a novel mutation in CRYBB1 gene in a Chinese family with autosomal dominant congenital cataract; results provide strong evidence that CRYBB1 is a pathogenic gene for congenital cataract

  9. This study has identified a novel nonsense mutation in CRYBB1 (p.Q223X) associated with autosomal dominant congenital nuclear cataract.

  10. These data suggest a mechanism whereby a transient disulfide bond occurs between alphaA- and betaB1-crystallin followed by a disulfide exchange with cysteine 49 of a neighboring alphaA-crystallin (show CRYAA Proteins) subunit.

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

  1. 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 (show CRYBA1 Proteins).

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

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

Crystallin, beta B1 (CRYBB1) Protein Profile

Protein 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 Proteins (CRYBB1)

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

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

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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