HSP70/HSC70 Antibody, Clone BB70

Cannot supply to this region.

SKU:: SMC-106
Additional Names:: HSPA1A, HSPA1B, HSPA1, HSPA8, HSP70, HSP70-1, HSP70.1, HSP70-2, HSP72, HSP73, HSC70, HSX70, Heat shock 70 kDa protein 1A, Heat shock 70 kDa protein 1B, Heat shock 70 kDa protein 8, Heat shock cognate 71 kDa protein
Application:: IHC, WB, IF, ICC, IP
Concentration:: 1 mg/ml
Species Reactivity:: Avian
Purification:: Protein G Purified
Storage Conditions:: -20[o]C
Supplier:: StressMarq Biosciences
Host:: Mouse
Reactivities:: Bovine, Canine, Fish, Hamster, Human, Mouse, Porcine, Rabbit, Rat, Yeast, Guinea Pig, Ovine, Insect/Arthropod
ABP:: IMP-GEN-2015-06 < 10% Serum <100ml
Buffer:: PBS pH7.2, 50% glycerol, 0.09% sodium azide
Immunogen:: Chicken HSP70/HSP90 complex
Clone:: BB70
Uniprot:: P08106
Synonyms:: dnaK-type molecular chaperone;heat shock 70 kDa protein;heat shock protein 70;HSP70
Extra Details:: HSP70 proteins are a highly conserved family of 70-kDa molecular chaperones essential for maintaining protein homeostasis across all domains of life. In eukaryotes, HSP70 genes form a multigene family, with isoforms localized to the cytosol, nucleus, mitochondria, endoplasmic reticulum, and chloroplasts. These chaperones are either constitutively expressed (HSC70) or stress-inducible (HSP70), and share over 50% sequence identity across species. Functionally, HSP70s bind ATP with high affinity and exhibit ATPase activity that is stimulated by interaction with unfolded or misfolded proteins. The N-terminal domain mediates ATP binding, while the C-terminal domain is responsible for substrate recognition. This ATP-driven cycle enables HSP70s to bind and release hydrophobic regions of nascent or damaged proteins, preventing aggregation and facilitating proper folding, transport, and assembly. In neuroscience, HSP70 and HSC70 are critical for neuronal survival under proteotoxic stress-conditions commonly associated with neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's disease. These chaperones stabilize misfolded proteins, support autophagic clearance, and modulate apoptotic signaling pathways. Their ability to interact with co-chaperones and degradation machinery further enhances their role in maintaining neuronal proteostasis. Given their central role in stress response and protein quality control, HSP70/HSC70 are promising therapeutic targets and biomarkers in neurodegeneration research.

Shipping Conditions:: Blue Ice