Product nameAnti-alpha A Crystallin/CRYAA antibody
See all alpha A Crystallin/CRYAA primary antibodies
DescriptionRabbit polyclonal to alpha A Crystallin/CRYAA
Tested applicationsSuitable for: WBmore details
Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat, Chimpanzee, Gorilla, Orangutan
Synthetic peptide corresponding to Human alpha A Crystallin/CRYAA aa 150 to the C-terminus (C terminal) conjugated to keyhole limpet haemocyanin.
Database link: P02489
- This antibody gave a positive signal in Human Brain and Spinal Cord tissue lysates.
This product was previously labelled as alpha A Crystallin
Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Batches of this product that have a concentration < 1mg/ml may have BSA added as a stabilising agent. If you would like information about the formulation of a specific lot, please contact our scientific support team who will be happy to help.
Concentration information loading...
PurityImmunogen affinity purified
Our Abpromise guarantee covers the use of ab139503 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||Use a concentration of 1 µg/ml. Detects a band of approximately 20 kDa (predicted molecular weight: 20 kDa).|
FunctionMay contribute to the transparency and refractive index of the lens.
Involvement in diseaseDefects in CRYAA are a cause of cataract autosomal dominant (ADC) [MIM:604219]. Cataract is 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. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. Cataract is the most common treatable cause of visual disability in childhood.
Sequence similaritiesBelongs to the small heat shock protein (HSP20) family.
modificationsO-glycosylated; contains N-acetylglucosamine side chains.
Deamidation of Asn-101 in lens occurs mostly during the first 30 years of age, followed by a small additional amount of deamidation (approximately 5%) during the next approximately 38 years, resulting in a maximum of approximately 50% deamidation during the lifetime of the individual.
Phosphorylation on Ser-122 seems to be developmentally regulated. Absent in the first months of life, it appears during the first 12 years of human lifetime. The relative amount of phosphorylated form versus unphosphorylated form does not change over the lifetime of the individual.
Cellular localizationCytoplasm. Nucleus. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
- Information by UniProt
- Acry 1 antibody
- Alpha crystallin A chain antibody
- Alpha-crystallin A chain antibody
All lanes : Anti-alpha A Crystallin/CRYAA antibody (ab139503) at 1 µg/ml
Lane 1 : Brain (Human) Tissue Lysate - adult normal tissue
Lane 2 : Spinal Cord (Human) Tissue Lysate - adult normal tissue
Lysates/proteins at 10 µg per lane.
All lanes : Donkey Anti-Rabbit IgG H&L preadsorbed (ab97081) at 1/10000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size: 20 kDa
Observed band size: 20 kDa
Additional bands at: 28 kDa (possible non-specific binding)
Exposure time: 30 seconds
This blot was produced using a 4-12% Bis-tris gel under the MES buffer system. The gel was run at 200V for 35 minutes before being transferred onto a Nitrocellulose membrane at 30V for 70 minutes. The membrane was then blocked for an hour using 5% Bovine Serum Albumin before being incubated with ab139503 overnight at 4°C. Antibody binding was detected using an anti-rabbit antibody conjugated to HRP, and visualised using ECL development solution.
ab139503 has not yet been referenced specifically in any publications.