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HSP70/HSP72 recombinant protein

HSP70/HSP72 (rat), (recombinant)

Gene Names
Hspa1a; HSP72; Hspa1; Hspa1b; Hsp70-1
Applications
Western Blot, Gel Super Shift Assay
Purity
>=90% (SDS-PAGE; Western blot)
Purified by multi-step chromatography
Synonyms
HSP70/HSP72; HSP70/HSP72 (rat); (recombinant); HSP70/HSP72 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Purity/Purification
>=90% (SDS-PAGE; Western blot)
Purified by multi-step chromatography
Form/Format
Liquid. In 50mM TRIS, pH7.5, containing 1.0mM DTT, 100mM sodium chloride, and 0.1mM PMSF
Applicable Applications for HSP70/HSP72 recombinant protein
Western Blot (WB), Proliferation assay, GST pulldown, Activity assay
Preparation and Storage
For long term storage, store at -80 degree C
Shipping: Shipped on Dry Ice
Related Product Information for HSP70/HSP72 recombinant protein
The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin -like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.
Product Categories/Family for HSP70/HSP72 recombinant protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
70,185 Da
NCBI Official Full Name
heat shock 70 kDa protein 1A/1B
NCBI Official Synonym Full Names
heat shock 70kD protein 1A
NCBI Official Symbol
Hspa1a
NCBI Official Synonym Symbols
HSP72; Hspa1; Hspa1b; Hsp70-1
NCBI Protein Information
heat shock 70 kDa protein 1A/1B; HSP70.1/2; HSP70-1/HSP70-2; heat shock protein 70-1; heat shock 70 kDa protein 1/2
UniProt Protein Name
Heat shock 70 kDa protein 1A
UniProt Gene Name
Hspa1a
UniProt Synonym Gene Names
Hsp70-1; Hspa1; HSP70-2; HSP70.2

NCBI Description

heat inducible gene; induced by global ischemia and kainic acid-induced seizures [RGD, Feb 2006]

Uniprot Description

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. 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. 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. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response.

Research Articles on HSP70/HSP72

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Product Notes

The HSP70/HSP72 hspa1a (Catalog #AAA565962) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. AAA Biotech's HSP70/HSP72 can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), Proliferation assay, GST pulldown, Activity assay. Researchers should empirically determine the suitability of the HSP70/HSP72 hspa1a for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "HSP70/HSP72, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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