Comparison

Anti-HSP70 Monoclonal Antibody European Partner

Item no. BOS-M00949-1
Manufacturer Boster
Amount 100 ug
Category
Type Antibody Monoclonal
Format Liquid
Applications WB, IF, IP, IHC, ICC
Clone 3A3
Specific against Human (Homo sapiens), Mouse (Murine, Mus musculus), Rat (Rattus norvegicus), Fish, Chicken (Gallus gallus domesticus), Drosophila, Bacteria (generic), Yeast (Saccharomyces cerevisiae)
Host Mouse
Isotype IgG1
ECLASS 10.1 42030590
ECLASS 11.0 42030590
UNSPSC 12352203
Alias HSP70 1, HSP70 2, HSP70.1, HSP72, HSP73, HSPA1, HSPA1A, HSPA1B
Available
Specificity Human,Mouse,Rat,Amphibians,Chicken,Fish,Yeast,Drosophila,Bacteria,Brine shrimp
Manufacturer - Category
Primary Antibodies, Monoclonal Antibodies, 2279
Storage Conditions
Store at -20°C for one year. Avoid repeated freeze-thaw cycles.
Clonality
Monoclonal
Application Details
WB (1:5000), ICC/IF (1:500), IP (2µg); optimal dilutions for assays should be determined by the user.
Manufacturer - Gene Name
HSP70
Background
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 (1). 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 (2). 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 (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). 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 (5). 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. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.
Immunogen
Human recombinant HSP70 overexpressed in E.coli
Contents
PBS pH 7.2, 50% glycerol, 0.09% sodium azide
Purification
Protein G Purified
Concentration
1 mg/ml
Manufacturer - Research Category
Cancer, Chaperones, Heat Shock Proteins, Protein Trafficking, Signal Transduction, Tumor Biomarkers
Protein Name
HSP70
Subcellular Localization
Cytoplasm
Short Description
Boster Bio Anti-HSP70 Monoclonal Antibody catalog # M00949-1. Tested in IP, IF, WB applications. This antibody reacts with Human, Mouse, Rat.
Description
Boster Bio Anti-HSP70 Monoclonal Antibody catalog # M00949-1. Tested in IP, IF, WB applications. This antibody reacts with Human, Mouse, Rat.

Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.

All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.

Amount: 100 ug
Available: In stock
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