C7990
Anti-phospho-α-B Crystallin (54-64) (pSer59) antibody produced in rabbit
affinity isolated antibody, lyophilized powder
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About This Item
Source biologique
rabbit
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
affinity isolated antibody
Type de produit anticorps
primary antibodies
Clone
polyclonal
Forme
lyophilized powder
Espèces réactives
rat, bovine, human
Technique(s)
indirect immunofluorescence: 8 μg/mL using human brain from Alexander′s diseased patients
western blot: 0.5 μg/mL using recombinant bovine phospho-α-B crystallin (Ser59)
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
phosphorylation (pSer59)
Informations sur le gène
human ... CRYAB(1410)
rat ... Cryab(25420)
Description générale
α-B-crystallin (CRYAB) belongs to small heat-shock protein family with chaperone-like function. Almost entire lens proteins composed of crystallins and within that α-crystallin accounts for 40% of total lens protein. α-Crystallin is composed of two primary gene products, α-A and α-B. α-B crystallin in particular, has been detected in many tissues in the central nervous system, and is considered to be a useful marker in a variety of neurodegenerative diseases.
Spécificité
This antibody does not detect the unphosphorylated form of the protein.
Immunogène
synthetic phosphopeptide: FLRAPS(p)WIDTG
Application
Anti-phospho-α-B Crystallin (54-64) (pSer59) antibody is suitable for indirect immunofluorescence in 8μg/mL using human brain from Alexander′s diseased patients. It is also suitable for western blot analysis in concentration of 0.5μg/mL using recombinant bovine phospho-α-B crystallin (Ser59).
Actions biochimiques/physiologiques
Anti-phospho-α-B Crystallin (54-64) (pSer59) antibody is responsible for the optical properties of the lens and have been identified from metabolic enzymes and stress proteins. In many neurological diseases, α B-crystallin have found over-expressed and any alterations in this protein leads cataract and myopathy. In addition to maintaining proper refractive index, it also functions in a chaperone-like manner by preventing the formation of aggregates possibly leading to cataract formation. It is believed that the phosphorylated states of α-crystallin occur in response to cellular stress and may serve a structural control function and play a role in protein maintenance.
Forme physique
Lyophilized from phosphate buffered saline, pH 7.4, with 3% bovine serum albumin and 0.05% sodium azide.
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Code de la classe de stockage
10 - Combustible liquids
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Suraj P Bhat
Progress in drug research. Fortschritte der Arzneimittelforschung. Progres des recherches pharmaceutiques, 60, 205-262 (2003-06-07)
Far from being a physical entity, assembled of inanimate structural proteins, the ocular lens epitomizes the biological ingenuity that sustains an essential and near-perfect physical system of immaculate optics. Crystallins (alpha, beta, and gamma) provide transparency by dint of their
Joseph Horwitz
Experimental eye research, 76(2), 145-153 (2003-02-05)
Alpha A and alpha B-crystallins are a major protein component of the mammalian eye lens. Being a member of the small heat-shock protein family they possess chaperone-like function. The alpha-crystallins and especially alpha B is also found outside the lens
Joram Piatigorsky
Journal of structural and functional genomics, 3(1-4), 131-137 (2003-07-03)
The crystallins account for 80-90% of the water-soluble proteins of the transparent lens. These diverse proteins are responsible for the optical properties of the lens and have been recruited from metabolic enzymes and stress proteins. They often differ among species
A F van Rijk et al.
Ophthalmologica. Journal international d'ophtalmologie. International journal of ophthalmology. Zeitschrift fur Augenheilkunde, 214(1), 7-12 (2000-02-05)
alphaB-Crystallin, which has homology with the small heat shock proteins, is the basic subunit of alpha-crystallin, a major component of the vertebrate eye lens. These crystallins have for a long time been thought to be absolutely lens specific. However, about
Franz Narberhaus
Microbiology and molecular biology reviews : MMBR, 66(1), 64-93 (2002-03-05)
Alpha-crystallins were originally recognized as proteins contributing to the transparency of the mammalian eye lens. Subsequently, they have been found in many, but not all, members of the Archaea, Bacteria, and Eucarya. Most members of the diverse alpha-crystallin family have
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