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Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Additionally we are shipping CRYAB Antibodies (510) and CRYAB Kits (52) and many more products for this protein.
Showing 10 out of 30 products:
Mechanistic studies revealed KLF4 (show KLF4 Proteins) specifically bound the promoter of CRYAB and upregulated CRYAB expression in human osteosarcoma cells.
mRNA levels of HSP family members (HSP70B', HSP72 (show HSPA1A Proteins), HSP40/DNAJ (show DNAJB1 Proteins), and HSP20 (show HSPB6 Proteins)/CRYAB) are upregulated by the intracellular MMP3 (show MMP3 Proteins) overload.
HspB5 maybe trigger the epithelial-mesenchymal transition in colorectal cancer (CRC (show CALR Proteins)) by activating the ERK (show EPHB2 Proteins) signaling pathway. It is a potential tumor biomarker for CRC (show CALR Proteins) diagnosis and prognosis.
The CLN6 (show CLN6 Proteins) is not only a molecular entity of the anti-aggregate activity conferred by the ER manipulation using TMalphaBC, but also serves as a potential target of therapeutic interventions.
Results demonstrated that CRYAA (show CRYAA Proteins) rs7278468 and CRYAB rs370803064/rs387907338 are correlated with the risk and clinicopathological features of children suffering from congenital cataract.
A missense mutation in alpha B-crystallin that changes proline 20 to an arginine leads to diminished anti-apoptotic activity compared with the native protein.
phosphorylation finely regulates the chaperone activity of CRYAB with multipass TMPs and suggest a pivotal role for S59 in this process
A missense mutation (p.D109G) in CRYAB causes restrictive cardiomyopathy (RCM (show Unc5c Proteins)).
This work examines the molecular mechanism by which two canonical sHsps, alphaB-crystallin (alphaB-c) and Hsp27 (show HSPB1 Proteins), interact with aggregation-prone alpha-syn to prevent its aggregation in vitro Both sHsps are very effective inhibitors of alpha-syn aggregation
343delT/343delT and WT KI/343delT-induced pluripotent stem cell-derived skeletal myotubes and cardiomyocytes did not express detectable levels of 343delT protein, contributable to the extreme insolubility of the mutant protein. Overexpression of HSPB5 343delT resulted in insoluble mutant protein aggregates and induction of a cellular stress response.
findings offer additional insight into the early transcriptional changes caused by Cryaa (show CRYAA Proteins) and Cryab 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
desmin and alphaBeta-crystallin are localized at sarcoplasmic reticulum (SR)-mitochondria-associated membranes (MAMs), where they interact with VDAC, Mic60 - the core component of mitochondrial contact site and cristae organizing system (MICOS) complex - and ATP synthase, suggesting that these associations could be crucial in mitoprotection at different levels.
This study demonstrated that HspB5 mRNA localization in myelin-enriched white and gray matter
alphaB-crystallin is an important regulator of epithelial-mesenchymal transition, acting as a molecular chaperone (show HSP90AA1 Proteins) for SMAD4 (show SMAD4 Proteins) and as its potential therapeutic target for preventing subretinal fibrosis development in neovascular age-related macular degeneration
It is a non-Hsp gene, which is essential for HSF1 (show HSF1 Proteins)-mediated maintenance of whole body homeostasis.
A previously unrecognized link between c-Jun (show JUN Proteins) and Nrf2 (show NFE2L2 Proteins) transcription factors and redox-induced CRYAB expression in muscle cells.
CryAB protects decidualization against stress conditions.
TNF-alpha (show TNF Proteins)-induced endothelial adhesion molecule (show NCAM1 Proteins) expression is reduced in inflamed vessels of alphaB-crystallin deficient mice, and leukocyte rolling velocity and IkappaB levels are increased.
Study shows that overexpression of Bcl-2 (show BCL2 Proteins) is sufficient to reduce the levels and overall architecture of protein deposition in the transgenic CryABR120G/Bcl-2 (show BCL2 Proteins) hearts.
alphaB-crystallin is over-expressed in fibrotic lung tissue and favors TGF-beta1 (show TGFB1 Proteins) pathway via its role in modulating the cellular localization of Smad4 (show SMAD4 Proteins).
The alphaB-crystallin content of bovine type I muscle fibers is quantitatively similar to that in the predominantly type I fibers of rat soleus muscle.
In the presence of alpha-crystallin or GroEL (show GroEL Proteins) the kinetic of GAPDH (show GAPDH Proteins) aggregation is changed from the diffusion-limited cluster-cluster aggregation to the reaction-limited cluster-cluster aggregation.
one of the functions of alphaB-crystallin is to bind microtubules via microtubule binding proteins and to give the MTs (show NEU2 Proteins) resistance to disassembly
The study provides evidence for the regulation of the chaperone activity of alphaB-crystallin by phosphorylation and indicates that this may play an important role in alleviating the pathogenic effects associated with protein conformational diseases.
This study clearly demonstrated that both the length and electrostatic charge of the COOH-terminal segment play crucial roles in governing the structural stability and chaperone activity of alphaB-crystallin.
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. Elevated expression of alpha-B crystallin occurs in many neurological diseases\; a missense mutation cosegregated in a family with a desmin-related myopathy.
alpha-crystallin B chain
, heat shock protein beta-5
, heat-shock 20 kD like-protein
, renal carcinoma antigen NY-REN-27
, rosenthal fiber component
, alpha B-crystallin
, crystallin, alpha 2
, Crystallin, alpha polypeptide 2
, hypothetical protein
, crystallin, alpha B
, alpha B crystallin
, crystallin, alpha polypeptide 2
, Alpha-crystallin B chain