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Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Additionally we are shipping Crystallin, alpha A Proteins (67) and Crystallin, alpha A Kits (14) and many more products for this protein.
Showing 10 out of 92 products:
Cow (Bovine) Monoclonal CRYAA Primary Antibody for ELISA, WB - ABIN361798
Bullard, Ferguson, Minajeva, Leake, Gautel, Labeit, Ding, Labeit, Horwitz, Leonard, Linke: Association of the chaperone alphaB-crystallin with titin in heart muscle. in The Journal of biological chemistry 2004
Show all 8 references for ABIN361798
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 references for ABIN1881229
Human Monoclonal CRYAA Primary Antibody for ELISA, WB - ABIN2477375
Andley, Mathur, Griest, Petrash: Cloning, expression, and chaperone-like activity of human alphaA-crystallin. in The Journal of biological chemistry 1997
Human Monoclonal CRYAA Primary Antibody for ELISA, WB - ABIN165392
Laksanalamai, Robb: Small heat shock proteins from extremophiles: a review. in Extremophiles : life under extreme conditions 2004
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.
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
alphaA-crystallin membrane insertion is oligomer-size dependent
isomerization of Asp (show ASIP Antibodies) might disrupt the higher order polymeric state of alpha-crystallin, resulting in decreased solubility and function, ultimately contributing to lens protein impairment and cataract formation with aging
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).
Similar to wild type alphaA- and alphaB-crystallins, the deamidated mutants showed strong interaction with betaA3-crystallin (show CRYBA1 Antibodies).
Identification of a novel mutation in CRYAA associated with congenital cataracts.
A novel disease-causing mutation, c.246_248delCGC (p.117delR), of the CRYAA gene has been identified in a Chinese family with autosomal-type perinuclear congenital cataracts.
The loss of interactions between alpha A-crystallin N-terminal mutants and alpha B-crystallin (show CRYAB Antibodies) signifies quaternary structural alterations due to mutation in the arginine residues.
CpG islands hypermethylation of alphaA-crystallin gene may be involved in nuclear cataract formation after pars (show EPRS Antibodies) plana vitrectomy.
Genetic variations of KCNAB1 (show KCNAB1 Antibodies) and CRYAA are associated with age-related nuclear cataract.
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.
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.
mouse lens epithelial cell progression through the cell cycle is significantly affected by expression of alphaA and alphaB-crystallin (show CRYAB Antibodies)
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).
crystallin, alpha A
, alpha-crystallin A chain
, alpha-A-crystallin protein
, alpha-crystallin A chain-like
, crystallin, alpha-1
, heat shock protein beta-4
, human alphaA-crystallin (CRYA1)
, Crystallin, alpha polypeptide A
, crystallin, alpha 1
, lens opacity 18
, alpha A crystallin
, Alpha-crystallin A chain