Recombinant Human HSP70/HSPA1A Protein, CF
Recombinant Human HSP70/HSPA1A Protein, CF Summary
HSP70/HSPA1A is a molecular chaperone that assists in the folding of nascent polypeptides and the refolding of denatured proteins, but can also promote their degradation in conjunction with specific E3 ligases, such as CHIP, if either of these processes proceeds inefficiently. Reaction conditions will need to be optimized for each specific application. We recommend an initial HSP70/HSPA1A concentration of 2-3 μM for in vitro use. IMPORTANT: HSP40/DNAJB1 (Catalog # AP-110), or another suitable co-chaperone, is required for HSP70/HSPA1A activity and should be used at a concentration that is equimolar to HSP70/HSPA1A.
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
X mg/ml (X μM) in 50 mM HEPES pH 8, 100 mM NaCl, 5 mM DTT
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Heat Shock 70kDa Protein (HSP70), also known as Heat Shock 70kDa Protein 1A (HSPA1A), is a 641 amino acid (aa) member of the HSP70 family of molecular chaperones with a predicted molecular weight of 70 kDa. Human HSP70/HSPA1A shares 95% and 97% aa sequence identity with the mouse and rat orthologs, respectively. It has an N-terminal nucleotide-binding domain, which contains ATPase activity, and a C-terminal substrate-binding domain (1). HSP70/HSPA1A promotes the proper folding of nascent polypeptides and assists in the refolding of denatured proteins (2). However, if either of these processes proceeds too slowly or fails, HSP70/HSPA1A can interact with the HSP40 co-chaperone protein and the CHIP/STUB1 Ubiquitin ligase (E3) to promote ubiquitination and degradation of the nascent polypeptide or denatured protein (3,4). HSP70/HSPA1A can be regulated post-translationally via multiple mechanisms, including phosphorylation, ubiquitination, and methylation (5-8). For example, unmethylated HSP70/HSPA1A localizes to the cytoplasm, but following methylation on Lys561 it is found only in the nucleus (8). Pathologically, HSP70/HSPA1A has been implicated in the promotion of multiple cancer types (8-10). Conversely, it is thought to protect against several neurodegenerative diseases that are caused by the accumulation of misfolded proteins (11,12).
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Citation for Recombinant Human HSP70/HSPA1A Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Toll-like receptor 4 signaling in trigeminal ganglion neurons contributes tongue-referred pain associated with tooth pulp inflammation.
Authors: Ohara, Kinuyo, Shimizu, Kohei, Matsuura, Shingo, Ogiso, Bunnai, Omagari, Daisuke, Asano, Masatake, Tsuboi, Yoshiyuk, Shinoda, Masamich, Iwata, Koichi
J Neuroinflammation, 2013;10(0):139.
Sample Types: Whole Tissue
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