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Merck

H1775

Monoclonal Anti-Heat Shock Protein 90 antibody produced in mouse

clone AC-16, ascites fluid

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A propos de cet article

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
MFCD02189140
Conjugate:
unconjugated
Clone:
AC-16, monoclonal
Application:
ARR, WB
Citations:
29

Principaux documents

Voir toute la documentation
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biological source

mouse

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.

P07900

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

200

Gene Information

human ... HSP90AA1(3320), HSP90AB1(3326)
mouse ... Hsp90aa1(15519), Hsp90ab1(15516)

Catégories apparentées

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.

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.
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.

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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Classe de stockage

12 - Non Combustible Liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificats d'analyse (COA)

Lot/Batch Number
0000458269
0000458269
0000294113
0000294113
0000199558

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Consulter la Bibliothèque de documents

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
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)
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)
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)
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