CRYAA anticorps (Atto 488)
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- Antigène Voir toutes CRYAA Anticorps
- CRYAA (Crystallin, alpha A (CRYAA))
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Reactivité
- Humain
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Hôte
- Souris
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Clonalité
- Monoclonal
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Conjugué
- Cet anticorp CRYAA est conjugé à/à la Atto 488
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Application
- Western Blotting (WB), ELISA, Immunofluorescence (IF), Immunocytochemistry (ICC)
- Specificité
- Detects ~20 kDa. Does not cross-react with αB-crystallin, βL-crystallin, ΒH- crystallin, γ-crystallin, HSP25, HSP27 or HSP47 proteins.
- Réactivité croisée
- Boeuf (Vache), Humain, Souris, Rat
- Purification
- Protein G Purified
- Immunogène
- Native Alpha Crystallin
- Clone
- 1H3-B8
- Isotype
- IgG1
- Top Product
- Discover our top product CRYAA Anticorps primaire
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- Indications d'application
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- WB (1:2000)
- ICC/IF (1:100)
- optimal dilutions for assays should be determined by the user.
- Commentaires
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0.5 μg/ml was sufficient for detection of 100 ng purified alphaA crystalline by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Concentration
- 1 mg/mL
- Buffer
- PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated
- Agent conservateur
- Sodium azide
- Précaution d'utilisation
- This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
- Stock
- 4 °C
- Stockage commentaire
- Conjugated antibodies should be stored at 4°C
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- Antigène
- CRYAA (Crystallin, alpha A (CRYAA))
- Autre désignation
- Alpha A Crystallin (CRYAA Produits)
- Sujet
- The alpha-crystallins are major water-soluble lens structural proteins of the vertebrate eye that are related to the small heat shock protein family. The alpha-crystallins possess structural and functional similarities with HSP25 and HSP27 (1). Mammalian lens cystallins are divided into alpha, beta and gamma families. Alpha and beta families are further divided into acidic and basic groups (Alpha-A and Alpha-B respectively). In the lens, alpha-crystallin primarily functions to maintain proper refractive index, however it can also function as a molecular chaperone that binds to the denatured proteins, keeping them in solution and thereby maintaining the translucency of the lens. When cellular stress occurs, alpha-crystallin enters its' phosphorylated state and may serve a structural control function and play a role in protein maintenance (2). In addition to their interaction with proteins, alpha-crystallins also interact with native molecules such as membrane proteins, Golgi matrix protein, structural proteins, nuclear proteins and DNA (3, 4, 5, 6, and 7). Two other functions are an autokinase activity and participation in the intracellular architecture, and it has also been proven that both alpha-A and B prevent apoptosis by inhibiting caspases (8).
- ID gène
- 1409
- NCBI Accession
- NP_000385
- UniProt
- P02489
- Pathways
- M Phase
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