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Key Documents

H7658

Sigma-Aldrich

Heat Shock Protein 25 from mouse

recombinant, expressed in E. coli, buffered aqueous solution, ≥90% (SDS-GE)

Sinonimo/i:

HSP 25

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About This Item

Codice UNSPSC:
12352202
NACRES:
NA.32

Origine biologica

mouse

Livello qualitativo

Ricombinante

expressed in E. coli

Saggio

≥90% (SDS-GE)

Forma fisica

buffered aqueous solution

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−70°C

Informazioni sul gene

mouse ... Hspb1(15507)

Applicazioni

Heat shock protein 25 from mouse has been used to prevent the degradation of proteins during sample preparation for proteome analysis.

Azioni biochim/fisiol

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).

Stato fisico

Solution in 20 mM Tris HCl, pH 7.5, 10 mM NaCl, 1 mM EDTA, 1 mM β-mercaptoethanol

Codice della classe di stoccaggio

10 - Combustible liquids


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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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