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AV44365

Sigma-Aldrich

Anti-PPIB (AB1) antibody produced in rabbit

IgG fraction of antiserum

Sinonimo/i:

Anti-CYP-S1, Anti-CYPB, Anti-MGC14109, Anti-MGC2224, Anti-Peptidylprolyl isomerase B (cyclophilin B), Anti-SCYLP

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About This Item

Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

IgG fraction of antiserum

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Forma fisica

buffered aqueous solution

PM

24 kDa

Reattività contro le specie

rabbit, human, mouse, guinea pig, dog

Concentrazione

0.5 mg - 1 mg/mL

tecniche

immunohistochemistry: suitable
western blot: suitable

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

wet ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... PPIB(5479)

Descrizione generale

The previously assigned protein identifier A8K534 has been merged into P23284. Full details can be found on the UniProt database.

Immunogeno

Synthetic peptide directed towards the middle region of human PPIB

Applicazioni

Anti-PPIB (AB1) antibody produced in rabbit is suitable for western blotting at a concentration of 5.0μg/ml and for immunohistochemistry of paraffin-embedded tissue sections at a concentration of 4-8μg/ml.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)

Azioni biochim/fisiol

Peptidylprolyl isomerase B (PPIB; cyclophilin B) is a protein released with secretory pathway in the biological fluids by the rough endoplasmic reticulum. It is involved in the regulation of cyclosporine A-mediated immunosuppression. Mutations in the PPIB gene cause a delay in procollagen chain association in osteoblasts that is one of the features of osteogenesis imperfecta phenotypes.

Sequenza

Synthetic peptide located within the following region: FITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIADC

Stato fisico

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Di Zhu et al.
Nature medicine, 21(6), 572-580 (2015-05-26)
B cell malignancies frequently colonize the bone marrow. The mechanisms responsible for this preferential homing are incompletely understood. Here we studied multiple myeloma (MM) as a model of a terminally differentiated B cell malignancy that selectively colonizes the bone marrow.
Fleur S van Dijk et al.
American journal of human genetics, 85(4), 521-527 (2009-09-29)
Deficiency of cartilage-associated protein (CRTAP) or prolyl 3-hydroxylase 1(P3H1) has been reported in autosomal-recessive lethal or severe osteogenesis imperfecta (OI). CRTAP, P3H1, and cyclophilin B (CyPB) form an intracellular collagen-modifying complex that 3-hydroxylates proline at position 986 (P986) in the
Shawna M Pyott et al.
Human molecular genetics, 20(8), 1595-1609 (2011-02-02)
Recessive mutations in the cartilage-associated protein (CRTAP), leucine proline-enriched proteoglycan 1 (LEPRE1) and peptidyl prolyl cis-trans isomerase B (PPIB) genes result in phenotypes that range from lethal in the perinatal period to severe deforming osteogenesis imperfecta (OI). These genes encode
Aileen M Barnes et al.
The New England journal of medicine, 362(6), 521-528 (2010-01-22)
Osteogenesis imperfecta is a heritable disorder that causes bone fragility. Mutations in type I collagen result in autosomal dominant osteogenesis imperfecta, whereas mutations in either of two components of the collagen prolyl 3-hydroxylation complex (cartilage-associated protein [CRTAP] and prolyl 3-hydroxylase

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