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SAB4300541

Sigma-Aldrich

Anti-HSP90AB1 (Ab-254) antibody produced in rabbit

affinity isolated antibody

Sinônimo(s):

Anti-D6S182 antibody produced in rabbit, Anti-FLJ26984 antibody produced in rabbit, Anti-HSP90-BETA antibody produced in rabbit, Anti-HSP90B antibody produced in rabbit, Anti-heat shock protein 90kDa alpha (cytosolic), class B member 1 antibody produced in rabbit

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About This Item

Número MDL:
MFCD07370344
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous solution

peso molecular

~92 kDa

reatividade de espécies

mouse, rat, human

concentração

1 mg/mL

técnica(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:50-1:100
indirect immunofluorescence: 1:100-1:200
western blot: 1:500-1:1000

Isotipo

IgG

sequência de imunogênio

(V-G-S-D-E)

nº de adesão NCBI

NP_031381.2

nº de adesão UniProt

P08238

Condições de expedição

wet ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... HSP90AB1(3326)

Descrição geral

HSP90AB1 (heat shock protein 90 αfamily class B member 1) belongs to the Hsp90 family. It consists of major members-Hsp90α, Hsp90β, GRP94 (glucose-regulated protein 94) and Hsp75. It is located on chromosome 6p21. It is an ATP-dependent molecular chaperone, that is of 90kDa.

Imunogênio

Peptide sequence around aa. 252-256 (V-G-S-D-E), according to the protein HSP90AB1.

Ações bioquímicas/fisiológicas

HSP90AB1 (heat shock protein 90 αfamily class B member 1) participates in signal transduction, protein folding and degradation, and morphological evolution. It is required for the transport of client proteins between the cytoplasm and nucleus. In lung adenocarcinoma patients, overexpression of HSP90AB1 in non-small cell lung cancer tissues results in imperfect clinical predictions. Suppression of this gene reduces the potential of endothelial cells to form tube structures.

Características e benefícios

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Descrição-alvo

Molecular chaperone. Has ATPase activity.

forma física

Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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A novel variant on chromosome 6p21.1 is associated with the risk of developing colorectal cancer: a two-stage case-control study in Han Chinese
Xu C, et al.
BMC Cancer, 16(1), 807-807 (2016)
[Hsp90AB1 Protein is Overexpressed in Non-small Cell Lung Cancer Tissues ?and Associated with Poor Prognosis in Lung Adenocarcinoma Patients]
Wang M, et al.
Zhongguo Fei ai za Zhi = Chinese Journal of Lung Cancer, 19(2), 64-69 (2016)
Valeria Capurro et al.
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Deletion of phenylalanine at position 508 (F508del) in the CFTR chloride channel is the most frequent mutation in cystic fibrosis (CF) patients. F508del impairs the stability and folding of the CFTR protein, thus resulting in mistrafficking and premature degradation. F508del-CFTR
Hsp90? promoted endothelial cell-dependent tumor angiogenesis in hepatocellular carcinoma
Meng J, et al.
Molecular Cancer, 16(1), 72-72 (2017)
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The ability to detect biomarkers with ultrahigh sensitivity radically transformed biology and disease diagnosis. However, owing to incompatibilities with infrastructure in current biological and medical laboratories, recent innovations in analytical technology have not received broad adoption. Here, we report a
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