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H1775

Sigma-Aldrich

Monoclonal Anti-Heat Shock Protein 90 antibody produced in mouse

clone AC-16, ascites fluid

Synonym(s):

Anti-EL52, Anti-HEL-S-65p, Anti-HSP86, Anti-HSP89A, Anti-HSP90A, Anti-HSP90N, Anti-HSPC1, Anti-HSPCA, Anti-HSPCAL1, Anti-HSPCAL4, Anti-HSPN, Anti-Hsp103, Anti-Hsp89, Anti-Hsp90, Anti-LAP-2, Anti-LAP2

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

AC-16, monoclonal

mol wt

antigen 88 kDa

contains

15 mM sodium azide

species reactivity

wheat germ, chicken, Sf9 cell line, rabbit, rat, human, mouse, Achlya

packaging

antibody small pack of 25 μL

technique(s)

microarray: suitable
western blot: 1:1,000 using cultured human foreskin fibroblasts

isotype

IgG2b

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

General description

HSP90AB1 (heat shock protein 90α family 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. HSP90AB1is an ATP-dependent molecular chaperone, having a molecular weight of 90kDa. HSP90AA1 is located on human chromosome 14q32.31.

Specificity

The antibody is reactive with both the constitutive and the inducible forms of HSP90. However, it does not bind to the native form of HSP90. It does not recognize HSP90 from E. coli and yeast.

Immunogen

heat shock protein 90 (HSP90) from the water mold Achlya ambisexualis

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunohistochemistry (1 paper)
Western Blotting (1 paper)
Monoclonal Anti-Heat Shock Protein 90 antibody has been used in ovarian histomorphology, immunohistochemistry and western blotting.

Biochem/physiol Actions

HSP90AB1 (heat shock protein 90α family 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.

Disclaimer

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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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Antioxidant and molecular chaperone defences during estivation and arousal in the South American apple snail Pomacea canaliculata
Giraud B M, et al.
The Journal of Experimental Biology, 216(4), 614-622 (2013)
Hsp90AB1 Protein is Overexpressed in Non-small Cell Lung Cancer Tissues and Associated with Poor Prognosis in Lung Adenocarcinoma Patients
Wang M, et al.
Chinese Journal of Analytical Chemistry, 19(2), 64-69 (2016)
t (3; 14)(q27; q32) HSP90AA1/BCL6
Huret J L.
Atlas of Genetics and Cytogenetics in Oncology and Haematology (2013)
X-S Liu et al.
Oncogene, 35(23), 3071-3078 (2015-10-13)
We recently reported that ZBTB7A is a bona fide transcription repressor of key glycolytic genes and its downregulation in human cancer contributes to tumor metabolism. As reduced expression of ZBTB7A is found only in a subset of human cancers, we
Exposure to chemical cocktails before or after conception-the effect of timing on ovarian development
Bellingham M, et al.
Molecular and Cellular Endocrinology, 376(1-2), 156-172 (2013)

Articles

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