生物源
rabbit
品質等級
共軛
unconjugated
抗體表格
affinity isolated antibody
抗體產品種類
primary antibodies
無性繁殖
polyclonal
形狀
lyophilized powder
物種活性
rat, bovine, human
技術
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登錄號
運輸包裝
dry ice
儲存溫度
−20°C
目標翻譯後修改
phosphorylation (pSer59)
基因資訊
human ... CRYAB(1410)
rat ... Cryab(25420)
一般說明
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.
特異性
This antibody does not detect the unphosphorylated form of the protein.
免疫原
synthetic phosphopeptide: FLRAPS(p)WIDTG
應用
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.
外觀
Lyophilized from phosphate buffered saline, pH 7.4, with 3% bovine serum albumin and 0.05% sodium azide.
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儲存類別代碼
10 - Combustible liquids
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
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
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
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
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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