生物来源
rabbit
质量水平
偶联物
unconjugated
抗体形式
affinity isolated antibody
抗体产品类型
primary antibodies
克隆
polyclonal
表单
lyophilized powder
种属反应性
rat, bovine, human
技术
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)
UniProt登记号
运输
dry ice
储存温度
−20°C
靶向翻译后修饰
phosphorylation (pSer59)
基因信息
human ... CRYAB(1410)
rat ... Cryab(25420)
一般描述
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.
免疫原
synthetic phosphopeptide: FLRAPS(p)WIDTG
应用
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).
生化/生理作用
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.
This antibody does not detect the unphosphorylated form of the protein.
外形
Lyophilized from phosphate buffered saline, pH 7.4, with 3% bovine serum albumin and 0.05% sodium azide.
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储存分类代码
10 - Combustible liquids
法规信息
新产品
此项目有
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
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
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
Hui Qin et al.
Medical oncology (Northwood, London, England), 31(8), 142-142 (2014-07-23)
Alpha B-crystallin (CRYAB) is one of the principal members of the small heat-shock protein family, and several studies described the CRYAB expression in human cancers. However, the association between CRYAB expression and the clinical features of non-small cell lung cancer
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