Ahsa1 (NM_146036) Mouse Recombinant Protein

CAT#: TP505046

Purified recombinant protein of Mouse AHA1, activator of heat shock protein ATPase 1 (Ahsa1), with C-terminal MYC/DDK tag, expressed in HEK293T cells, 20ug

Product Images

Purified recombinant protein Ahsa1 was analyzed by SDS-PAGE gel and Coomossie Blue Staining.

Specifications

Product Data

• Species: Mouse
• Expression Host: HEK293T
• Expression cDNA Clone or AA Sequence:
  Protein Sequence

  >MR205046 protein sequence
  Red=Cloning site Green=Tags(s)
  
  MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTEKLKTLFLAVRVENEEGKCEVTEVNKLDGEASI
  NNRKGKLIFFYEWTIKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEDG
  VKLLREAVGIYISTLKTEFTQGMILPTVNGESVDPVGQPALKTETCKAKSAPSKSQAKPVGVKIPTCKIT
  LKETFLTSPEELYRVFTTQELVQAFTHAPAALEADRGGKFHMVDGNVTGEFTDLVPEKHIAMKWRFKSWP
  EGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
  
  TRTRPLEQKLISEEDLAANDILDYKDDDDKV
• Tag: C-MYC/DDK
• Predicted MW: 38.1 kDa
• Concentration: >0.05 µg/µL as determined by microplate BCA method
• Purity: > 80% as determined by SDS-PAGE and Coomassie blue staining
• Buffer: 25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol
• Note: For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process.
• Storage: Store at -80°C after receiving vials.
• Stability: Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.

Reference Data

• RefSeq: NP_666148
• Locus ID: 217737
• UniProt ID: Q8BK64
• Cytogenetics: 12 D2
• Refseq Size: 1330
• Refseq ORF: 1017
• Synonyms: BC023857; p38
• Summary: Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (By similarity). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155).[UniProtKB/Swiss-Prot Function]