Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Crystallins are the dominant structural components of the vertebrate eye lens. Zusätzlich bieten wir Ihnen Crystallin, beta A1 Antikörper (45) und Crystallin, beta A1 Proteine (12) und viele weitere Produktgruppen zu diesem Protein an.
Showing 1 out of 3 products:
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.
association between a frameshift mutation in exon 6 of CRYBA1/A3 and congenital cataracts
Data indicate that alpha-crystallin B chain (zeige CRYAB ELISA Kits) and beta-crystallin A3-cyrstallins dissociate to the monomers upon racemization of d-aspartic acids (Asp (zeige ASIP ELISA Kits)).
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 (zeige CRYBB1 ELISA Kits) homomers and the betaA3/betaB1-crystallin (zeige CRYBB1 ELISA Kits) 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.
Data show that betaA3/A1-crystallin affects the signal transducer and activator of transcription 3 (STAT3 (zeige STAT3 ELISA Kits)) activation in optic nerve astrocytes.
loss of CRYBA1 causes lysosomal dysregulation leading to the impairment of both autophagy and phagocytosis
p53 (zeige TP53 ELISA Kits) 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.
crystallin, beta A4
, crystallin, beta A1
, beta-crystallin A3
, beta-crystallin A1
, beta A1-crystallin
, beta A3-crystallin
, crystallin, beta A3
, eye lens structural protein
, beta-A3 crystallin
, beta-A3/A1 crystalline
, beta A3 crystallin
, lens structural protein