HSP70, Recombinant Protein

Heat shock 70 kDa protein 1; HSPA1A; HSPA1; HSPA1B; HSP70; HSP70.1; HSP70-1/HSP70-2; Heat shock 70 kDa protein 1; Heat shock 70 kDa protein 1; heat shock 70kDa protein 1A

For Research Use Only. Not for use in diagnostic procedures.

E Coli

> 95% by SDS-PAGE

Liquid. 20mM Tris-HCI buffer(pH7.5), containing 2mM DTT

1 mg/ml (determined by Bradford assay) (lot specific)

Can be stored at 2 degree C to 8 degree C.
For long term storage, aliquot and store at -20° C or -80°C.
Avoid repeated freezing and thawing cycles.

Small volumes of HSP70 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Hsp70 is a human heat shock protein. Hsp70 is an important part of the cell's machinery for protein folding, and help to protect cells from stress. In most species, there are many proteins that belong to the hsp70 family. Some of these are only expressed under stress conditions, while some are present in cells under normal growth conditions and are not heat-inducible. They can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc...). Recombinant human Hsp70, fused to His-tag at N-terminus, was expressed in E Coli and purified by using conventional chromatography techniques.

Heat Shock Proteins

SDS-PAGE

72.2kDa (661aa), confirmed by MALDI-TOF.

heat shock protein family A (Hsp70) member 1A

heat shock 70 kDa protein 1A

Heat shock 70 kDa protein 1A

; HSP70.1  [Similar Products]

This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401).

Gething M-J, et al. (1992). Nature. 355. 33-45; Lewis MJ, et al. EMBO J. (1985) 4:3137-3143

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