385059
HSP70, acetylated (Lys77) (DnaK Type Molecular Chaperone HSP70 1, Epididymis Secretory Protein Li 103, Heat Shock 70kD Protein 1, Heat Shock 70kD Protein 1/2, Heat Shock 70kD Protein 1A/1B, Heat Shock 70kD Protein 1A, Heat Shock 70kD Protein 1B, Heat Shock Induced Protein, HEL S 103, HSP70 1, HSP70 1B, HSP70 2, HSP70-1/HSP70-2, HSP70-1A, HSP70.1, HSP70.1/HSP70.2, HSP70I, HSP71 HUMAN, HSP72, HSPA1, HSPA1A, HSPA1B)
Size
£590.00
- SKU:
- 385059
- Purity:
- Purified by peptide affinity chromatography.
- Storage Conditions:
- -20°C
- Supplier:
- United States Biological
- Host:
- Rabbit
- Immunogen:
- Synthetic peptide corresponding to aa1-100 of human HSP70 at N-terminal, conjugated to KLH.
- Format:
- Supplied as a liquid in PBS, pH 7.4, 0.09% sodium azide, 50% glycerol.
- Extra Details:
- HSP70 genes encode abundant heat-inducible 70kD HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 50% identity (2). The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kD which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport. Alpha-Synuclein (SNCA) is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals (1). Alpha-synuclein is highly expressed in the mitochondria of the olfactory bulb, hippocampus, striatum and thalamus (2). Functionally, it has been shown to significantly interact with tubulin (3), and may serve as a potential microtubule-associated protein. It has also been found to be essential for normal development of the cognitive functions; inactivation may lead to impaired spatial learning and working memory (4). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimers disease amyloid plaque, and a major component of Lewy body inclusions, and Parkinson’s disease. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin (5, 6). Alpha synuclein phosphorylated at serine 129 constitutes 90% of the alpha synuclein found in Lewy bodies (7, 8). Applications: Suitable for use in Western Blot, ELISA, Immunocytochemistry/Immunofluorescence. Other applications not tested. Recommended Dilution: Western Blot: 1:1000 Immunocytochemistry/Immunofluorescence: 1:60 ELISA: 1:1000 Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
- Shipping Conditions:
- Blue Ice