Activator of 90 kDa heat shock protein ATPase homolog 1 Recombinant Protein | AHSA1 recombinant protein

Recombinant Human Activator of 90 kDa heat shock protein ATPase homolog 1

Cat. Num. AAA717061

• Gene Names: AHSA1; p38; AHA1; C14orf3
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Activator of 90 kDa heat shock protein ATPase homolog 1; Recombinant Human Activator of 90 kDa heat shock protein ATPase homolog 1; p38; AHSA1 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 1-338aa; Full Length
• Sequence: MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
• Sequence Length: 338

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for AHSA1 recombinant protein

Cochaperone that stimulates HSP90 ATPase activity. May affect a step in the endoplasmic reticulum to Golgi trafficking.

Product Categories/Family for AHSA1 recombinant protein

Neuroscience

References

Isolation of a novel gene underexpressed in Down syndrome.Michaud J., Chrast R., Rossier C., Papassavas M.P., Antonarakis S.E., Scott H.S.Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning.Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence and analysis of human chromosome 14.Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.Nature 421:601-607(2003)

NCBI and Uniprot Product Information

• NCBI GI #: 6912280
• NCBI GeneID: 10598
• NCBI Accession #: NP_036243.1
• NCBI GenBank Nucleotide #: NM_012111.2
• UniProt Accession #: O95433; Q96IL6; Q9P060; B2R9L2; B4DUR9
• Molecular Weight: 65.3 kDa
• NCBI Official Full Name: activator of 90 kDa heat shock protein ATPase homolog 1
• NCBI Official Synonym Full Names: AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast)
• NCBI Official Symbol: AHSA1
• NCBI Official Synonym Symbols: p38; AHA1; C14orf3
• NCBI Protein Information: activator of 90 kDa heat shock protein ATPase homolog 1
• UniProt Protein Name: Activator of 90 kDa heat shock protein ATPase homolog 1
• Protein Family: Activator of 90 kDa heat shock protein ATPase
• UniProt Gene Name: AHSA1
• UniProt Synonym Gene Names: C14orf3; AHA1
• UniProt Entry Name: AHSA1_HUMAN

Uniprot Description

AHSA1: Cochaperone that stimulates HSP90 ATPase activity. May affect a step in the endoplasmic reticulum to Golgi trafficking. Belongs to the AHA1 family.

Protein type: Chaperone

Chromosomal Location of Human Ortholog: 14q24

Cellular Component: cytoplasm; cytosol; endoplasmic reticulum

Molecular Function: ATPase activator activity; chaperone binding; protein binding

Biological Process: positive regulation of ATPase activity; response to stress