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CRYBA1

CRYBA1 (Crystallin Beta A1) is a Protein Coding gene. Diseases associated with CRYBA1 include Cataract 10, Multiple Types and Cataract 25. Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and structural constituent of eye lens. An important paralog of this gene is CRYBA4.
Full Name
Crystallin Beta A1
Function
Crystallins are the dominant structural components of the vertebrate eye lens.
Biological Process
Lens development in camera-type eye Source: GO_Central
Negative regulation of cytokine production Source: Ensembl
Negative regulation of ERK1 and ERK2 cascade Source: Ensembl
Negative regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
Negative regulation of protein kinase B signaling Source: Ensembl
Negative regulation of TOR signaling Source: Ensembl
Positive regulation of anoikis Source: Ensembl
Visual perception Source: UniProtKB
Cellular Location
Nucleus; Cytoplasm
Involvement in disease
Cataract 10, multiple types (CTRCT10):
An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. CTRCT10 includes congenital zonular with sutural opacities, among others. This is a form of zonular cataract with an erect Y-shaped anterior and an inverted Y-shaped posterior sutural opacities. Zonular or lamellar cataracts are opacities, broad or narrow, usually consisting of powdery white dots affecting only certain layers or zones between the cortex and nucleus of an otherwise clear lens. The opacity may be so dense as to render the entire central region of the lens completely opaque, or so translucent that vision is hardly if at all impeded. Zonular cataracts generally do not involve the embryonic nucleus, though sometimes they involve the fetal nucleus. Usually sharply separated from a clear cortex outside them, they may have projections from their outer edges known as riders or spokes.
PTM
Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility.
S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental.

Anti-CRYBA1 antibodies

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Target: CRYBA1
Host: Mouse
Antibody Isotype: IgG1
Specificity: Cattle
Clone: CBCNC-376
Application*: WB
Target: CRYBA1
Host: Rabbit
Antibody Isotype: IgG
Specificity: Human, Mouse, Rat
Clone: BA0376
Application*: WB
Target: CRYBA1
Host: Rabbit
Antibody Isotype: IgG
Specificity: Human, Mouse, Rat
Clone: BA0377
Application*: IF, IP, WB
More Infomation
For Research Use Only. Not For Clinical Use.
(P): Predicted
* Abbreviations
IFImmunofluorescence
IHImmunohistochemistry
IPImmunoprecipitation
WBWestern Blot
EELISA
MMicroarray
CIChromatin Immunoprecipitation
FFlow Cytometry
FNFunction Assay
IDImmunodiffusion
RRadioimmunoassay
TCTissue Culture
GSGel Supershift
NNeutralization
BBlocking
AActivation
IInhibition
DDepletion
ESELISpot
DBDot Blot
MCMass Cytometry/CyTOF
CTCytotoxicity
SStimulation
AGAgonist
APApoptosis
IMImmunomicroscopy
BABioassay
CSCostimulation
EMElectron Microscopy
IEImmunoelectrophoresis
PAPeptide Array
ICImmunocytochemistry
PEPeptide ELISA
MDMeDIP
SHIn situ hybridization
IAEnzyme Immunoassay
SEsandwich ELISA
PLProximity Ligation Assay
ECELISA(Cap)
EDELISA(Det)
BIBioimaging
IOImmunoassay
LFLateral Flow Immunoassay
LALuminex Assay
CImmunohistochemistry-Frozen Sections
PImmunohistologyp-Paraffin Sections
ISIntracellular Staining for Flow Cytometry
MSElectrophoretic Mobility Shift Assay
RIRNA Binding Protein Immunoprecipitation (RIP)
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