Human AHA1 Protein (Highly Pure)

<strong>Human AHA1 Protein (Highly Pure)</strong>_x000D_ <strong>Catalog number:</strong> B2011544_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 100 µg_x000D_ <strong>Molecular Weight or Concentration:</strong> 1 mg/mL_x000D_ <strong>Supplied as:</strong> Solution_x000D_ <strong>Applications:</strong> molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> -20℃_x000D_ <strong>Keywords:</strong>_x000D_ AHA1 protein, Purified recombinant Human AHA1 protein, Hsp90 co-chaperone AHA1 protein, AHA1 protein, Activator of Hsp90 ATPase protein 1 protein, HSPC322 protein, AHA-1 protein, p38., AHSA 1 protein, AHA1, Activator of heat shock 90kDa protein ATPase homolog 1 protein, AHA 1 protein, AHA 1, 19-337) protein,_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Oroz J, Blair LJ, Zweckstetter M. Dynamic Aha1 co-chaperone binding to human Hsp90 Protein Sci. 2019 Sep;28(9):1545-1551._x000D_ 2: Heider M, Eichner R, Stroh J, Morath V, Kuisl A, Zecha J, Lawatscheck J, Baek K, Garz AK, Rudelius M, Deuschle FC, Keller U, Lemeer S, Verbeek M, Götze KS, Skerra A, Weber WA, Buchner J, Schulman BA, Kuster B, Fernández-Sáiz V, Bassermann F. The IMiD target CRBN determines HSP90 activity toward transmembrane proteins essential in multiple myeloma Mol Cell. 2021 Mar 18;81(6):1170-1186.e10._x000D_ 3: Hu H, Wang Q, Du J, Liu Z, Ding Y, Xue H, Zhou C, Feng L, Zhang N. Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity Molecules. 2021 Mar 30;26(7):1943._x000D_ 4: Singh JK, Hutt DM, Tait B, Guy NC, Sivils JC, Ortiz NR, Payan AN, Komaragiri SK, Owens JJ, Culbertson D, Blair LJ, Dickey C, Kuo SY, Finley D, Dyson HJ, Cox MB, Chaudhary J, Gestwicki JE, Balch WE. Management of Hsp90-Dependent Protein Folding by Small Molecules Targeting the Aha1 Co-Chaperone Cell Chem Biol. 2020 Mar 19;27(3):292-305.e6._x000D_ 5: Rehn AB, Buchner J. p23 and Aha1 Subcell Biochem. 2015;78:113-31._x000D_ 6: Kim D, Moon JW, Min DH, Ko ES, Ahn B, Kim ES, Lee JY. AHA1 regulates cell migration and invasion via the EMT pathway in colorectal adenocarcinomas Sci Rep. 2021 Oct 7;11(1):19946._x000D_ 7: Zheng D, Liu W, Xie W, Huang G, Jiang Q, Yang Y, Huang J, Xing Z, Yuan M, Wei M, Li Y, Yin J, Shen J, Shi Z. AHA1 upregulates IDH1 and metabolic activity to promote growth and metastasis and predicts prognosis in osteosarcoma Signal Transduct Target Ther. 2021 Jan 20;6(1):25._x000D_ 8: Wolfgeher D, Dunn DM, Woodford MR, Bourboulia D, Bratslavsky G, Mollapour M, Kron SJ, Truman AW. The dynamic interactome of human Aha1 upon Y223 phosphorylation Data Brief. 2015 Nov 6;5:752-5._x000D_ 9: Edkins AL. CHIP: a co-chaperone for degradation by the proteasome Subcell Biochem. 2015;78:219-42._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/18281495">10: Holmes JL, Sharp SY, Hobbs S, Workman P. Silencing of HSP90 cochaperone AHA1 expression decreases client protein activation and increases cellular sensitivity to the HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin Cancer Res. 2008 Feb 15;68(4):1188-97. </a>_x000D_ _x000D_ <strong>Products Related to Human AHA1 Protein (Highly Pure) can be found at</strong> <a href="https://moleculardepot.com/product-category/Proteins/"> Proteins</a>