HSP70/HSPA1A Antibody (N27F3-4)

Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eucaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eucaryotes 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 5O% identity. 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. When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa 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. 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. 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.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 3 applications: FLOW, Flow-CS, WB.

Showing Publications 1 - 3 of 3.

Publications using NB110-96425	Applications	Species
Berner J, Miebach L, Kordt M et al. Chronic oxidative stress adaptation in head and neck cancer cells generates slow-cyclers with decreased tumour growth in vivo British journal of cancer 2023-07-17 [PMID: 37460712] (Flow-CS, Human)	Flow-CS	Human
Leermakers PA, Remels AHV, Zonneveld MI et al. Iron deficiency-induced loss of skeletal muscle mitochondrial proteins and respiratory capacity; the role of mitophagy and secretion of mitochondria-containing vesicles FASEB J. 2020-03-23 [PMID: 32202346] (WB, Mouse)	WB	Mouse
Freund E, Liedtke KR, Miebach L et al. Identification of Two Kinase Inhibitors with Synergistic Toxicity with Low-Dose Hydrogen Peroxide in Colorectal Cancer Cells in vitro Cancers (Basel). [PMID: 31906582] (FLOW, Mouse)	FLOW	Mouse

Array NB110-96425

• HSP70/HSPA1A Antibodies
• HSP70/HSPA1A Lysate
• HSP70/HSPA1A Proteins
• HSP70/HSPA1A ELISAs
• HSP70/HSPA1A Proteins and Enzyme