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Human Polyclonal CRYAA Primary Antibody for WB - ABIN1881229
Deng, Chen, Xie, Zhao, Gong, Liu, Zhang, Sun, Liu, Ma, Batra, Li: The small heat shock protein alphaA-crystallin is expressed in pancreas and acts as a negative regulator of carcinogenesis. in Biochimica et biophysica acta 2010
Show all 4 Pubmed References
Low crystallin alpha a expression is associated with pancreatic tumorigenesis.
The results suggest that the N-terminal domain of CRYAA is required during in vitro complex formation with filensin (show BFSP1 Antibodies) and phakinin (show BFSP2 Antibodies).
CRYAA polymorphism is a genetic marker of inter-individual differences in the risk of nuclear ARC (show NOL3 Antibodies).
Results demonstrated that CRYAA rs7278468 and CRYAB (show CRYAB Antibodies) rs370803064/rs387907338 are correlated with the risk and clinicopathological features of children suffering from congenital cataract.
These mutations revealed a range of detrimental effects on the structure, stability and functional properties of aA-Cry (show CRY2 Antibodies) which all together can explain the pathomechanisms underlying development of the associated congenital cataract disorders
The study demonstrates that residues 70-88 in CRYAA act as a primary substrate binding site and account for the bulk of the total chaperone activity.
The T allele of rs7278468 in the crystallin alpha A promoter is associated with age-related cataract through increasing binding of KLF-10 (show KLF10 Antibodies) and thus decreasing crystallin alpha A transcription.
The evidence presented suggests that the methylation of the CpG sites of the CRYAA promotor directly affect Sp1 (show PSG1 Antibodies) binding, leading to down expression of CRYAA in human lens epithelial cells.
The p.R21Q mutation of CRYAA is the most likely cause of paediatric cataract in this family.
these results suggest that individuals carrying the alphaA-Crystallin R12C mutation are at an increased risk to develop early-onset cataract under condition of oxidative stress
findings offer additional insight into the early transcriptional changes caused by Cryaa and Cryab (show CRYAB Antibodies) mutations associated with autosomal dominant cataracts, and indicate that the transcript levels of certain genes are affected by the expression of mutant alpha-crystallin in vivo
Collectively, these studies show that FGF signaling up-regulates expression of alphaA-crystallin both directly and indirectly via up-regulation of c-Maf (show MAF Antibodies).
Knockout of alphaA-crystallin inhibited pathologic neovascularization through the VEGF (show VEGFA Antibodies) and VEGFR2 (show KDR Antibodies) signaling pathways both in vitro and in vivo.
p53 (show TP53 Antibodies) can regulate lens differentiation by controlling expression of the differentiation genes coding for the lens crystallins.
Alpha A crystallin is a moonlighting protein that functions as a heat shock protein as well as a lens crystalline.
alphaA-crystallin may protect against geographic atrophy.
alphaA and alphaB regulate caspase-3 (show CASP3 Antibodies) and Bax (show BAX Antibodies) in vitro and in vivo to regulate lens differentiation.
these findings show that mutation of alphaA-crystallin induces activation of the UPR during cataract formation.
Hydroimidazolone modification of human alphaA-crystallin: Effect on the chaperone function and protein refolding ability.
Methionine oxidation of alpha-crystallin in combination with loss of MsrA (show MSR1 Antibodies) repair causes loss of alpha-crystallin chaperone function.
For moderate O-GlcNAcylation on bovine crystalline alpha, the preferred amino acids were Pro > Ala > Gly at position -2, Ala > Thr (show TRH Antibodies) >Val > Lys (show LYZ Antibodies) > Pro at position -1, and Ala > Gly > Arg > Glu (show DCTN1 Antibodies) at position +2.
Alpha-crystallin, in the presence of the sorbitol dehydrogenase (SDH (show SORD Antibodies)) pyridine cofactor NAD(H), can exert a remarkable chaperone action by favoring the recovery of the enzyme activity from chemically denaturated SDH (show SDS Antibodies) up to 77%.
Conserved triad in alphaA-crystallin contributes to stability of higher order oligomers but is not essential for formation of tetramers.
Mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin, betaB2- and gammaS-(betaS)-crystallins.
The ontogeny and localization of the alphaA-crystallin and betaB1-crystallin (show CRYBB1 Antibodies) during embryonic lens development and regeneration indicated a different development program, although they have identical origins, the ectoderm.
The normal development observed in alphaA-crystallin deficient zebrafish embryos may reflect similarly non-essential roles for this protein in the early stages of both zebrafish and mammalian lens development.
Fndings establish that the C-terminal extension of alphaA crystallin can be either 3D domain swapped or non-3D domain swapped.
alphaA-crystallin (HSPB4) is expressed during development.
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. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone\; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits\; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed\; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC).
alpha-crystallin A chain
, crystallin, alpha-1
, heat shock protein beta-4
, human alphaA-crystallin (CRYA1)
, crystallin, alpha 1
, lens opacity 18
, alpha A crystallin
, alpha-A-crystallin protein
, alpha-crystallin A chain-like
, Crystallin, alpha polypeptide A
, crystallin, alpha A
, Alpha-crystallin A chain