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SAB4300541

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

affinity isolated antibody

Synonym(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

UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
MFCD07370344

Key Documents

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Product Name

Anti-HSP90AB1 (Ab-254) antibody produced in rabbit, affinity isolated antibody

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

~92 kDa

species reactivity

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

immunogen sequence

(V-G-S-D-E)

NCBI accession no.

NP_031381.2

UniProt accession no.

P08238

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

100

Gene Information

human ... HSP90AB1(3326)

Biochem/physiol Actions

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.

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.

Features and Benefits

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.

General description

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.
Molecular chaperone. Has ATPase activity.

Immunogen

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

Physical form

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

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Storage Class

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

常规特殊物品
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Certificates of Analysis (COA)

Lot/Batch Number
951421290

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Valeria Capurro et al.
International journal of molecular sciences, 22(10) (2021-06-03)
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
[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)
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)
Hsp90? promoted endothelial cell-dependent tumor angiogenesis in hepatocellular carcinoma
Meng J, et al.
Molecular Cancer, 16(1), 72-72 (2017)
Trehalose attenuates abdominal aortic aneurysm formation by inducing autophagy in smooth muscle cells.
Jiang, et al.
Journal of geriatric cardiology : JGC, 20, 214-222 (2023)
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