CA1023
Anti-Hsp90α Mouse mAb (EMD-17D7)
liquid, clone EMD-17D7, Calbiochem®
Synonyme(s) :
Anti-Heat Shock Protein 90α
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About This Item
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41
Produits recommandés
Source biologique
mouse
Niveau de qualité
Forme d'anticorps
purified antibody
Type de produit anticorps
primary antibodies
Clone
EMD-17D7, monoclonal
Forme
liquid
Contient
≤0.1% sodium azide as preservative
Espèces réactives
human
Fabricant/nom de marque
Calbiochem®
Conditions de stockage
OK to freeze
avoid repeated freeze/thaw cycles
Isotype
IgG1
Conditions d'expédition
wet ice
Température de stockage
−20°C
Modification post-traductionnelle de la cible
unmodified
Description générale
Protein G PLUS/protein A purified mouse monoclonal antibody. Recognizes the ~90 kDa Hsp90α protein.
Recognizes the ~90 kDa Hsp90α protein in HeLa cells. Does not recognize Hsp90β.
This Anti-Hsp90α Mouse mAb (EMD-17D7) is validated for use in ELISA, Immunoblotting, Immunoprecipitation for the detection of Hsp90α.
Immunogène
Hsp90α, His•Tag, Human, Recombinant (Cat. No. 385901)
Human
Application
ELISA (see comments)
Immunoblotting (1 g/ml)
Immunoprecipitation (5 g/0.7 mg protein)
Conditionnement
Please refer to vial label for lot-specific concentration.
Avertissement
Toxicity: Irritant (B)
Forme physique
In PBS.
Reconstitution
Following initial thaw, aliquot and freeze (-20°C).
Remarque sur l'analyse
Positive Control
H460 and HeLa cells
H460 and HeLa cells
Autres remarques
Detects native and recombinant Hsp90α. Does not recognize Hsp90β. This antibody will also work for ELISA, but concentration is assay dependent. Antibody should be titrated for optimal results in individual systems.
Scheibel, T., et al. 1999. Proc. Natl. Acad. Sci. USA96, 1297.
Nemoto, T., et al. 1997 J. Biol. Chem.272, 26179.
Nemoto, T., et al. 1998. Biochem. J.330, 989.
Nemoto, T., et al. 1997 J. Biol. Chem.272, 26179.
Nemoto, T., et al. 1998. Biochem. J.330, 989.
Informations légales
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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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.
Julian D Gillmore et al.
Journal of the American Society of Nephrology : JASN, 20(2), 444-451 (2008-12-17)
Mutations in the fibrinogen A alpha-chain gene are the most common cause of hereditary renal amyloidosis in the United Kingdom. Previous reports of fibrinogen A alpha-chain amyloidosis have been in isolated kindreds, usually in the context of a novel amyloidogenic
Priyamvada Jayaprakash et al.
Journal of cell science, 128(8), 1475-1480 (2015-03-05)
When tissues are injured and blood vessels clot, the local environment becomes ischemic, meaning that there is a lack of adequate supply of oxygen and glucose delivered to the surrounding cells. The heat shock protein-90 (Hsp90) family proteins protect tissues
Hang-Ming Dong et al.
Respiratory research, 18(1), 111-111 (2017-06-01)
The disruption and hyperpermeability of bronchial epithelial barrier are closely related to the pathogenesis of asthma. House dust mite (HDM), one of the most important allergens, could increase the airway epithelial permeability. Heat shock protein (Hsp) 90α is also implicated
Xin Tang et al.
Scientific reports, 9(1), 15108-15108 (2019-10-24)
Extracellular heat shock protein-90alpha (eHsp90α) plays an essential role in tumour invasion and metastasis. The plasma eHsp90α levels in patients with various cancers correlate with the stages of the diseases. Nonetheless, the mechanism of action by tumour-secreted eHsp90α remained unclear.
Jiacong Guo et al.
Molecular and cellular biology, 37(19) (2017-07-05)
Secreted exosomes carrying lipids, proteins, and nucleic acids conduct cell-cell communications within the microenvironment of both physiological and pathological conditions. Exosome secretion is triggered by extracellular or intracellular stress signals. Little is known, however, about the signal transduction between stress
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