HSP70 Recombinant Protein | HSPA1A recombinant protein

HSP70 Protein, Mouse, Recombinant (His Tag)

Cat. Num. AAA8123261

• Gene Names: Hspa1a; Hsp72; hsp68; Hsp70-3; Hsp70.3; hsp70A1
• Purity: >95% as determined by SDS-PAGE
• Synonyms: HSP70; HSP70 Protein; Mouse; Recombinant (His Tag); Mouse HSP70 Protein (His Tag); hsp68 Protein; Hsp70-3 Protein; Hsp70.3 Protein; hsp70A1 Protein; Hsp72 Protein; heat shock 70kDa protein 1A; HSPA1A recombinant protein

• Host: HEK293 Cells
• Purity/Purification: >95% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Ala2-Asp641

• Species: Mouse
• Endotoxin: <1.0EU per ug protein as determined by the LAL method.
• Predicted N Terminal: Met
• Tag: N-His
• Protein Construction: A DNA sequence encoding the mouse HSPA1A (NP_034609.2)(Ala2-Asp641) was expressed with a polyhistidine tag at the N-terminus.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

SDS-Page

Related Product Information for HSPA1A recombinant protein

Background: HSPA1A is a member of the Hsp70 protein family. The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP is synthesized intracellularly, which may protect cells from protein denaturation or death. Extracellularly, HSP can serve a cytokine function to initiate both innate and adaptive immunity through activation of APC. HSP serves also a chaperone function and facilitates the presentation of antigen peptide to T cells. Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulate their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp70 chaperones use the same mechanism of ATP-driven polypeptide binding and release.

Product Categories/Family for HSPA1A recombinant protein

Death Receptor Signaling

References

Heck TG, et al. (2011) HSP70 expression: does it a novel fatigue signalling factor from immune system to the brain Cell Biochem Funct. 29 (3): 215-26.Chen T, et al. (2010) Stress for maintaining memory: HSP70 as a mobile messenger for innate and adaptive immunity. Eur J Immunol. 40 (6): 1541-4.Young JC. (2010) Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol. 88 (2): 291-300.

NCBI and Uniprot Product Information

• NCBI GI #: 124339829
• NCBI GeneID: 193740
• NCBI Accession #: NP_034609.2
• NCBI GenBank Nucleotide #: NM_010479.2
• UniProt Accession #: Q61696; Q61697; Q7TQD8; Q9QWJ5
• Molecular Weight: 70,079 Da
• NCBI Official Full Name: heat shock 70 kDa protein 1A
• NCBI Official Synonym Full Names: heat shock protein 1A
• NCBI Official Symbol: Hspa1a
• NCBI Official Synonym Symbols: Hsp72; hsp68; Hsp70-3; Hsp70.3; hsp70A1
• NCBI Protein Information: heat shock 70 kDa protein 1A
• UniProt Protein Name: Heat shock 70 kDa protein 1A
• Protein Family: HSP70 co-chaperone
• UniProt Gene Name: Hspa1a
• UniProt Synonym Gene Names: Hsp70-3; Hsp70A1; HSP70.3

Uniprot Description

In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation.