Western Blot: HSP70/HSPA1A Antibody (C92F3A-5) [NB110-61582] - analysis of Human cell lysates from various cell lines showing detection of Hsp70 protein using Mouse Anti-Hsp70 Monoclonal Antibody, Clone C92. Load: 15 ug ...read more
Immunohistochemistry-Paraffin: HSP70/HSPA1A Antibody (C92F3A-5) [NB110-61582] - Tissue: colon carcinoma. Species: Human. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody at 1:10000 for 12 hours ...read more
Flow Cytometry: HSP70/HSPA1A Antibody (C92F3A-5) [NB110-61582] - Fluorescence Activated Cell Sorting analysis using Mouse Anti-Hsp70: FITC Monoclonal Antibody, Clone C92 (SMC-100). Tissue: Heat Shocked CD3+ CD8+ T ...read more
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
PBS (pH 7.4) and 50% Glycerol
0.1% Sodium Azide
Protein G purified
Alternate Names for HSP70/HSPA1A Antibody (C92F3A-5)
dnaK-type molecular chaperone HSP70-1
Heat shock 70 kDa protein 1/2
heat shock 70 kDa protein 1A/1B
heat shock 70kD protein 1A
heat shock 70kDa protein 1A
heat shock-induced protein
Hsp70 genes encode abundant heat-inducible 70-kDa 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 hsp70 (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 (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.
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.
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Bio-Techne appreciates the critical role that you and our products and services play in research efforts to further scientific innovation and discovery. We are continually assessing our manufacturing and supplier capabilities during the COVID-19 situation and are implementing precautionary measures to ensure uninterrupted supply of products and services. Currently, and as we abide by local shelter in place orders across the world, we are fully operational and do not anticipate any material supply disruptions across our Bio-Techne brands and product lines. As the situation evolves, our goal is to utilize preventive measures to reduce the threat that COVID-19 poses to our ability to meet the needs of our customers globally.