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C7990

Sigma-Aldrich

Anti-phospho-α-B Crystallin (54-64) (pSer59) antibody produced in rabbit

affinity isolated antibody, lyophilized powder

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

lyophilized powder

Speziesreaktivität

rat, bovine, human

Methode(n)

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-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

phosphorylation (pSer59)

Angaben zum Gen

human ... CRYAB(1410)
rat ... Cryab(25420)

Allgemeine Beschreibung

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.

Spezifität

This antibody does not detect the unphosphorylated form of the protein.

Immunogen

synthetic phosphopeptide: FLRAPS(p)WIDTG

Anwendung

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).

Biochem./physiol. Wirkung

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.

Physikalische Form

Lyophilized from phosphate buffered saline, pH 7.4, with 3% bovine serum albumin and 0.05% sodium azide.

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Lagerklassenschlüssel

10 - Combustible liquids


Analysenzertifikate (COA)

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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
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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