H7658
Heat Shock Protein 25 from mouse
recombinant, expressed in E. coli, buffered aqueous solution, ≥90% (SDS-GE)
Synonyme(s) :
HSP 25
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About This Item
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
mouse
Niveau de qualité
Produit recombinant
expressed in E. coli
Pureté
≥90% (SDS-GE)
Forme
buffered aqueous solution
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
mouse ... Hspb1(15507)
Application
Heat shock protein 25 from mouse has been used to prevent the degradation of proteins during sample preparation for proteome analysis.
Actions biochimiques/physiologiques
HSP25 (heat shock protein 25) from mouse is a chaperone which is required for cell protection, chemo-resistance, tumorigenicity, protection from cell death. Absence of HSP25 in mouse impairs wound healing rate. HSP25 is also referred to as HSPB1 (heat shock protein β-1).
Forme physique
Solution in 20 mM Tris HCl, pH 7.5, 10 mM NaCl, 1 mM EDTA, 1 mM β-mercaptoethanol
Code de la classe de stockage
10 - Combustible liquids
Certificats d'analyse (COA)
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Yasuhiro Kuramitsu et al.
Anticancer research, 35(6), 3217-3221 (2015-05-31)
Tumor progression is one of the most serious issues to overcome cancer disease. As a model of inflammation-induced tumor progression, we used the regressive murine fibrosarcoma cell clone QR-32 and the progressive malignant clone QRsP-11, that was derived from QR-32.
Denise I Jacobs et al.
Fungal genetics and biology : FG & B, 46 Suppl 1, S141-S152 (2008-10-01)
The filamentous fungus Aspergillus niger is widely exploited for industrial production of enzymes and organic acids. An integrated genomics approach was developed to determine cellular responses of A. niger to protein production in well-controlled fermentations. Different protein extraction methods in
Jonathan Crowe et al.
PloS one, 8(10), e77383-e77383 (2013-10-22)
There is large literature describing in vitro experiments on heat shock protein (hsp)B1 but understanding of its function in vivo is limited to studies in mice overexpressing human hspB1 protein. Experiments in cells have shown that hspB1 has chaperone activity
K Engel et al.
Biomedica biochimica acta, 50(9), 1065-1071 (1991-01-01)
A hybrid protein containing the N-terminal part of the murine stress protein hsp25 (amino acids 1 to 110) and the C-terminal part of the human stress protein hsp27 (amino acids 111 to 208) was expressed in E. coli using a
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