Tag/Conjugate
Unconjugated
Alternative Names
The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.
Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.
Antigen Description
The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]
Function
ATP binding; ATPase activity; MHC class II protein complex binding; TPR domain binding; TPR domain binding; identical protein binding; nitric-oxide synthase regulator activity; nucleotide binding; poly(A) RNA binding; protein binding; protein homodimeriza
Synonyms
HSP90AA1; heat shock protein 90kDa alpha (cytosolic), class A member 1; EL52; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; LAP-2; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; heat shock protein HSP 90-alpha; HSP 86; heat shock 86 kDa; LPS-associated protein 2; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; renal carcinoma antigen NY-REN-38; heat shock 90kD protein, alpha-like 4; epididymis luminal secretory protein 52; heat shock 90kD protein 1, alpha-like 4; lipopolysaccharide-associated protein 2;
Citations
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Herskowitz, JH; Seyfried, NT; et al. Phosphoproteomic Analysis Reveals Site-Specific Changes in GFAP and NDRG2 Phosphorylation in Frontotemporal Lobar Degeneration. JOURNAL OF PROTEOME RESEARCH 9:6368-6379(2010).
Negroni, L; Taouji, S; et al. Integrative Quantitative Proteomics Unveils Proteostasis Imbalance in Human Hepatocellular Carcinoma Developed on Nonfibrotic Livers. MOLECULAR & CELLULAR PROTEOMICS 13:3473-3483(2014).