| Product Name |
Recombinant Human Heat Shock 70kDa 6 (HSPA6) Protein |
| Product Overview |
This recombinant human Heat Shock 70kDa 6 (HSPA6) protein includes amino acids 1-387aa of the target gene is expressed in E.coli.The protein is supplied in lyophilized form and formulated in phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5% trehaloseprior to lyophilization. |
| Target Uniprot Id |
P17066 |
| Recommended Name |
Heat shock 70 kDa protein 6 |
| Gene Name |
HSPA6 |
| Synonyms |
Heat shock 70 kDa protein 6, HSPA6' |
| Species |
Human |
| Predicted Molecular Mass |
46 kDa |
| Expression System |
E.coli |
| Expression Range |
1-387aa |
| Tag |
N-6His |
| Purity |
>85% |
| Formulation |
Lyophilized |
| Buffer |
Phosphate buffered saline (pH7.4) containing 0.01% sarcosyl, 5%Trehalose |
| Storage Condition |
1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C. |
| Reconstitution Instruction |
Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%. |
| Applications |
Positive Control; Immunogen; SDS-PAGE; WB |
| Research Area |
Cancer |
| Target Function |
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 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. |
| Protein Family |
Heat shock protein 70 family |
