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Key Documents

SAB4300541

Sigma-Aldrich

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

affinity isolated antibody

Synonyme(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

Numéro MDL:
MFCD07370344
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

~92 kDa

Espèces réactives

mouse, rat, human

Concentration

1 mg/mL

Technique(s)

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

Isotype

IgG

Séquence immunogène

(V-G-S-D-E)

Numéro d'accès NCBI

NP_031381.2

Numéro d'accès UniProt

P08238

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... HSP90AB1(3326)

Description générale

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.

Immunogène

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

Actions biochimiques/physiologiques

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.

Caractéristiques et avantages

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.

Description de la cible

Molecular chaperone. Has ATPase activity.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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)
Hsp90? promoted endothelial cell-dependent tumor angiogenesis in hepatocellular carcinoma
Meng J, et al.
Molecular Cancer, 16(1), 72-72 (2017)
Junwei Li et al.
Nature biomedical engineering, 1 (2017-10-31)
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
Masashi Fukuoka et al.
PloS one, 9(7), e103130-e103130 (2014-07-30)
Heat shock, sudden change in temperature, triggers various responses in cells for protecting the cells from such a severe circumstance. Here we investigated gene silencing mediated by endogenous microRNAs (miRNAs) in mammalian cells exposed to a mild hyperthermia, by means
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