Crystallin, beta A1 Proteins (CRYBA1)

Crystallins are the dominant structural components of the vertebrate eye lens.. Additionally we are shipping Crystallin, beta A1 Antibodies (52) and Crystallin, beta A1 Kits (4) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
CRYBA1 1411 P05813
CRYBA1 12957  
CRYBA1 25583 P14881
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Top Crystallin, beta A1 Proteins at antibodies-online.com

Showing 8 out of 12 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
Insect Cells Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 50 Days
$6,749.58
Details
Insect Cells Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 50 Days
$6,749.58
Details
Wheat germ Human GST tag 10 μg Log in to see 11 to 12 Days
$325.44
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HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Log in to see 11 Days
$547.80
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Yeast Cow His tag   1 mg Log in to see 60 to 71 Days
$2,531.83
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Yeast Rat His tag   1 mg Log in to see 60 to 71 Days
$2,531.83
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Yeast Chicken His tag   1 mg Log in to see 60 to 71 Days
$2,531.83
Details
Escherichia coli (E. coli) Mouse T7 tag,His tag 100 μg Log in to see 15 to 18 Days
$704.00
Details

CRYBA1 Proteins by Origin and Source

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

More Proteins for Crystallin, beta A1 (CRYBA1) Interaction Partners

Human Crystallin, beta A1 (CRYBA1) interaction partners

  1. A recurrent DeltaG91CRYBA1/A3 mutation occurs independently in 6.4% of the Chinese families with autosomal dominant nuclear cataracts and most likely represents a mutational hot spot, which underscores the relations between nonprogressive nuclear cataract and CRYBA1/A3.

  2. We identified a de novo in-frame 3-bp deletion in the proband with an autosomal dominant congenital cataract, but not in her parents, in an Iranian family. This mutation has occurred de novo on a paternal gamete during spermatogenesis. The in-silico results predicted the interaction of CRYBA1 protein with the other CRY as well as proteins responsible for eye cell signaling.

  3. The findings suggest that impaired endolysosomal signaling in ocular astrocytes can cause PFV disease, by adversely affecting the vascular remodeling processes essential to ocular development, including regression of the fetal vasculature. [review]

  4. association between a frameshift mutation in exon 6 of CRYBA1/A3 and congenital cataracts

  5. Data indicate that alpha-crystallin B chain and beta-crystallin A3-cyrstallins dissociate to the monomers upon racemization of d-aspartic acids (Asp).

  6. A novel splice site mutation in CRYBA1/A3 is associated with autosomal dominant nuclear cataracts in a Chinese family.

  7. A splice site mutation (c.215+1G>A) at the first base of intron 3 of the crystallin beta A3/A1 (CRYBA3/A1) gene has been identified in Chinese congenital polymorphic cataract patients.

  8. ThebetaA3-crystallin and betaB1-crystallin homomers and the betaA3/betaB1-crystallin heteromer all undergo similar five-state folding pathways which include one dimeric and two monomeric intermediates.

  9. A G-->T splice site mutation of CRYBA1/A3 associated with autosomal dominant suture cataracts in a Chinese family.

  10. The c.279-281delGAG mutation in CRYBA1 is responsible for the autosomal dominant congenital nuclear cataract disease in this Chinese family.

  11. A serine-type protease activity of betaA3-crystalllin was responsible for its autodegradation.

  12. This is the first report of a phenotype of progressive nuclear and cortical cataracts related to the CRYBA3/A1 mutation IVS3+1 G>A.

  13. Mutations involved in congenital cataracts and deamidation in aged lenses commonly altered protein-protein interaction between human lens betaA3-crystallins.

  14. This study is the first report relating a mutation of CRYBA1/A3 to posterior polar cataract.

  15. A deletion mutation in the betaA1/A3 crystallin gene is associated with autosomal dominant congenital nuclear cataract

  16. comprehensive description of the biophysical consequences of a mutant beta-crystallin protein that is associated with human inherited cataract.

  17. The DeltaG91 mutation in CRYBA3/A1 is associated with an autosomal dominant congenital nuclear lactescent cataract

  18. The glutamine residues at the Q180 and the Q85 were substituted with glutamic acid residues by site-directed mutagenesis. These structural changes led to decreased stability during unfolding in urea and increased precipitation during heat denaturation.

  19. Delta91 mutation arise in a relatively mutation-prone sequence of the CRYBA1 gene.

  20. This study confirmed the interactions between a low molecular weight peptide derived from betaA3/A1-crystallin found in aged and cataract lenses and alphaB-crystallin.

Mouse (Murine) Crystallin, beta A1 (CRYBA1) interaction partners

  1. CRYbetaA3/A1-crystallin has a role in preventing nuclear cataract impaired lysosomal cargo clearance and calpain activation

  2. Data suggest a mechanism by which betaA3/A1-crystallin regulates lysosomal function by modulating the activity of V-ATPase.

  3. Data show that betaA3/A1-crystallin affects the signal transducer and activator of transcription 3 (STAT3) activation in optic nerve astrocytes.

  4. loss of CRYBA1 causes lysosomal dysregulation leading to the impairment of both autophagy and phagocytosis

  5. p53 can regulate lens differentiation by controlling expression of the differentiation genes coding for the lens crystallins.

  6. The thermodynamic consequences of the loss of beta A3-crystallin terminal extensions by in vivo proteolytic processing could increase their tendency to associate and so promote the formation of higher order associates in the aging and cataractous lens.

Cow (Bovine) Crystallin, beta A1 (CRYBA1) interaction partners

  1. Results show that both betaB2- and betaA3-crystallin bind calcium with moderate affinity.

Crystallin, beta A1 (CRYBA1) Protein Profile

Protein Summary

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

Gene names and symbols associated with Crystallin, beta A1 Proteins (CRYBA1)

  • crystallin beta A1 (CRYBA1)
  • crystallin, beta A1 (Cryba1)
  • crystallin, beta A1a (cryba1a)
  • crystallin beta A1 L homeolog (cryba1.L)
  • crystallin beta A1 (cryba1)
  • crystallin beta A1 (Cryba1)
  • crystallin, beta A1b (cryba1b)
  • BA3/A1 protein
  • BA3A1C protein
  • beta-A3 protein
  • Cryb protein
  • cryb1 protein
  • cryba1 protein
  • CRYBA3 protein
  • CTRCT10 protein
  • zgc:92688 protein
  • zgc:92720 protein

Protein level used designations for Crystallin, beta A1 Proteins (CRYBA1)

beta-crystallin A3 , crystallin, beta A3 , eye lens structural protein , beta-A1-crystallin , beta-A3/A1-crystallin , beta-crystallin A1 , beta-A3 crystallin , beta A3 crystallin , lens structural protein , crystallin, beta A1 , beta-A3/A1 crystalline , betaA3-crystallin , beta A1-crystallin , beta A3-crystallin , crystallin, beta A1b

GENE ID SPECIES
1411 Homo sapiens
12957 Mus musculus
25583 Rattus norvegicus
282202 Bos taurus
396499 Gallus gallus
436683 Danio rerio
468199 Pan troglodytes
491178 Canis lupus familiaris
494645 Xenopus laevis
716819 Macaca mulatta
100125179 Xenopus (Silurana) tropicalis
100379565 Cavia porcellus
100229047 Taeniopygia guttata
100519211 Sus scrofa
436859 Danio rerio
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