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Crystallins are the dominant structural components of the vertebrate eye lens. Additionally we are shipping Crystallin, beta A1 Proteins (12) and Crystallin, beta A1 Kits (2) and many more products for this protein.
Showing 10 out of 44 products:
Human Polyclonal CRYBA1 Primary Antibody for EIA, IHC (p) - ABIN950651
Xu, Wong, Tan, Jing, Zhou, Song: Decreasing the homodimer interaction: a common mechanism shared by the deltaG91 mutation and deamidation in betaA3-crystallin. in Molecular vision 2010
Show all 5 references for ABIN950651
Human Polyclonal CRYBA1 Primary Antibody for IHC (p), WB - ABIN656311
Gupta, Srivastava: Identification of interaction sites between human betaA3- and alphaA/alphaB-crystallins by mammalian two-hybrid and fluorescence resonance energy transfer acceptor photobleaching methods. in The Journal of biological chemistry 2009
Cow (Bovine) Polyclonal CRYBA1 Primary Antibody for WB - ABIN2784755
Müller, Distl: Linkage and association analyses of intragenic SNPs in the canine beta-crystallin genes CRYBB1, CRYBB2, CRYBB3, CRYBA1 and CRYBA4 with primary cataracts in wire-haired Dachshunds. in Animal genetics 2008
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 (show CRY2 Antibodies) as well as proteins responsible for eye cell signaling.
association between a frameshift mutation in exon 6 of CRYBA1/A3 and congenital cataracts
Data indicate that alpha-crystallin B chain (show CRYAB Antibodies) and beta-crystallin A3-cyrstallins dissociate to the monomers upon racemization of d-aspartic acids (Asp (show ASIP Antibodies)).
A novel splice site mutation in CRYBA1/A3 is associated with autosomal dominant nuclear cataracts in a Chinese family.
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.
ThebetaA3-crystallin and betaB1-crystallin (show CRYBB1 Antibodies) homomers and the betaA3/betaB1-crystallin (show CRYBB1 Antibodies) heteromer all undergo similar five-state folding pathways which include one dimeric and two monomeric intermediates.
A G-->T splice site mutation of CRYBA1/A3 associated with autosomal dominant suture cataracts in a Chinese family.
The c.279-281delGAG mutation in CRYBA1 is responsible for the autosomal dominant congenital nuclear cataract disease in this Chinese family.
This is the first report of a phenotype of progressive nuclear and cortical cataracts related to the CRYBA3/A1 mutation IVS3+1 G>A.
This study is the first report relating a mutation of CRYBA1/A3 to posterior polar cataract.
CRYbetaA3/A1-crystallin has a role in preventing nuclear cataract impaired lysosomal cargo clearance and calpain activation
Data suggest a mechanism by which betaA3/A1-crystallin regulates lysosomal function by modulating the activity of V-ATPase (show ATP6V1H Antibodies).
Data show that betaA3/A1-crystallin affects the signal transducer and activator of transcription 3 (STAT3 (show STAT3 Antibodies)) activation in optic nerve astrocytes.
loss of CRYBA1 causes lysosomal dysregulation leading to the impairment of both autophagy and phagocytosis
p53 (show TP53 Antibodies) can regulate lens differentiation by controlling expression of the differentiation genes coding for the lens crystallins.
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.
Results show that both betaB2- and betaA3-crystallin bind calcium with moderate affinity.
Crystallins are the dominant structural components of the vertebrate eye lens.
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, beta A3-crystallin
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, eye lens structural protein
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