HSP70 Protein

Cannot supply to this region.

SKU:: SPR-117
Additional Names:: HSPA1A, HSPA1B, HSPA1, HSP70, HSP70-1, HSP70.1, HSP70-2, HSP72, HSP73, HSX70, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1B
Application:: ELISA, SDS-PAGE, WB, FuncS
Molecular Weight:: ~70 kDa
Purity:: >90%
Purification:: Multi-step Purified
Storage Conditions:: -20[o]C
Supplier:: StressMarq Biosciences
ABP:: No Import Docs
Buffer:: 50mM Tris/HCl pH7.5, 0.3M NaCl, 10% glycerol, 0.1mM EDTA
Immunogen:: HSP70 Protein
Species:: Human
Sequence:: MAKAAAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTGASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVGYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSCIPPAPGVPQIEVTFDIDANGILNVTATKDSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD
Uniprot:: P0DMV8, P0DMV9
Synonyms:: dnaK-type molecular chaperone HSP70-1;epididymis secretory protein Li 103;epididymis secretory sperm binding protein;heat shock 70 kDa protein 1;heat shock 70 kDa protein 1/2;heat shock 70 kDa protein 1A;heat shock 70 kDa protein 1A/1B;Heat shock 70 kDa protein 1B;Heat shock 70 kDa protein 2;heat shock 70kD protein 1A;heat shock 70kD protein 1B;heat shock 70kDa protein 1A;heat shock 70kDa protein 1B;heat shock-induced protein;HEL-S-103;HSP70-1;HSP70-1/HSP70-2;HSP70-1A;HSP70-1B;HSP70-2;HSP70.1;HSP70.1/HSP70.2;HSP70.2;HSP70I;HSP72;HSPA1;HSX70
Extra Details:: HSP70 is a highly inducible molecular chaperone that plays a pivotal role in protein quality control across all major cellular compartments. In the brain, HSP70 is essential for preventing the aggregation of misfolded proteins, a key pathological feature of neurodegenerative diseases. HSP70 binds to nascent and partially folded polypeptides, stabilizing them and facilitating proper folding or directing them toward degradation pathways. This function is particularly critical in conditions such as Alzheimer's, Parkinson's, and ALS, where protein aggregation and impaired proteostasis drive neuronal dysfunction and cell death. The chaperone activity of HSP70 is regulated by ATP binding and hydrolysis, which triggers conformational changes that control substrate binding and release. Its ability to recognize hydrophobic regions of unfolded proteins enables it to suppress aggregation and promote cellular recovery from stress. Therapeutic strategies aimed at enhancing HSP70 expression or activity are under investigation for their potential to reduce neurotoxicity, improve protein clearance, and slow disease progression in neurodegenerative disorders.

Shipping Conditions:: Blue Ice