Comparison

Heat Shock Protein 70 (HSP70, HSP72, Hsc70, Heat Shock Cognate 70kD)

Item no. USB-136787
Manufacturer United States Biological
Amount 100 ug
Category
Type Antibody Monoclonal
Format Liquid
Applications WB, ELISA
Clone 5G1-95
Specific against Mouse (Murine, Mus musculus)
Host Mouse
Isotype IgG1
Purity Purified by Protein G affinity chromatography.
ECLASS 10.1 42030590
ECLASS 11.0 42030590
UNSPSC 12352203
Shipping Condition Cool pack
Available
Manufacturer - Type
Mab
Manufacturer - Category
Antibodies / Antibodies-Heat Shock Proteins
Shipping Temperature
Blue Ice
Storage Conditions
-20°C
Grade
Affinity Purified
Form
Supplied as a liquid in PBS, pH 7.4, 0.09% azide, 50% glycerol.
EU Commodity Code
30021010
Immunogen
Phaseolus aureus (mung bean)
Specificity
Recognizes constitutive and inducible plant Hsp70 (Hsc70/Hsp72) at ca.70kD. Does not cross-react with human, rat, bacteria (DNAKK) or human BIP.
Description
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 5O% 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 44kD 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.

Applications:
Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilution:
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 at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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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