Recombinant humaan AHA1-eiwit

The co-chaperone Aha1 (Activator of HSP90 ATPase-1) binds the middle domain of Hsp90 (amino acid 272-627) and is proposed to function as an ATPase-activating protein that competes with p23 and other co-chaperones for Hsp90 binding. Recombinant Aha1 was expressed in E. coli and purified by using conventional chromatography techniques.

Activator of Hsp90 ATPase-1 (AHA1, 19-337), AHA1, AHSA1, Activator of Hsp90 ATPase protein 1, Hsp90 co-chaperone AHA1, Activator of Hsp90 ATPase-1 Activator of 90 kDa heat shock protein ATPase homolog 1, Activator of heat shock 90kDa protein ATPase homolog 1, C14orf3, HSPC322, p38

E.coli

Human

Non-Tagged

SDS-PAGE

1 mg/mL (determined by Bradford assay)

< 1 EU per 1ug of protein (determined by LAL method)

> 95% by SDS-PAGE

36.1 kDa (320aa) confirmed by MALDI-TOF

Activator of Hsp90 ATPase1, AHA1, Activator of Hsp90 ATPase-1, AHA1, Activator of Hsp90 ATPase-1 (AHA1, 19-337), Activator of Hsp90 ATPase protein 1, Hsp90 co-chaperone AHA1, Activator of Hsp90 ATPase-1 Activator of 90 kDa heat shock protein ATPase homolog 1, Activator of heat shock 90kDa protein ATPase homolog 1, AHA 1, AHSA 1, AHSA1, C14orf3, HSPC322, p38., AHA0701-10 µg, AHA0701-20 µg, AHA0701-50 µg, AHA0701-100 µg, AHA0701-250 µg, AHA0701-500 µg, AHA0701-1 mg, AHA0701-10, AHA0701-20, AHA0701-50, AHA0701-100, AHA0701-250, AHA0701-500, AHA0701-1

Meyer P., et al (2004) . EMBO 23 (6) : 1402-10; ; Siligardi G., et al (2004) . J Biol Chem. 270 (50) : 51989-98;

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 2mM EDTA

Heat Shock Proteins

NP_036243

O95433

Human

MATNVNNWHW TERDASNWST DKLKTLFLAV QVQNEEGKCE VTEVSKLDGE ASINNRKGKL IFFYEWSVKL NWTGTSKSGV QYKGHVEIPN LSDENSVDEV EISVSLAKDE PDTNLVALMK EEGVKLLREA MGIYISTLKT EFTQGMILPT MNGESVDPVG QPALKTEERK AKPAPSKTQA RPVGVKIPTC KITLKETFLT SPEELYRVFT TQELVQAFTH APATLEADRG GKFHMVDGNV SGEFTDLVPE KHIVMKWRFK SWPEGHFATI TLTFIDKNGE TELCMEGRGI PAPEEERTRQ GWQRYYFEGI KQTFGYGARL