Heat Shock Protein 70 (HSP70)

Referência H1831-06-200ug

Tamanho : 200ug

Marca : US Biological

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H1831-06 Heat Shock Protein 70 (HSP70)

Clone Type
Polyclonal
Host
rabbit
Source
rat
Swiss Prot
P63018
Isotype
IgG
Grade
Affinity Purified
Applications
IHC WB
Crossreactivity
Bo Ca Ch Dr Gp Hm Hu Mk Mo Po Rb Rt Sh Ye
Shipping Temp
Blue Ice
Storage Temp
-20°C

The heat shock protein, Hsp70 is part of the Hsp70 family that contains a number of highly-related protein isoforms ranging in size from 66 kD to 78 kD. The 70 kD heat shock cognate protein, Hsc70 is closely related biochemically and biologically to Hsp70 and is part of the Hsp70 family. These proteins include both cognate members that are found within major intracellular compartments and highly inducible isoforms that appear to be predominantly cytoplasmic or nuclear in distribution (2). Members of the Hsp70 family are molecular chaperones which are involved in many cellular functions such as protein folding, transport, maturation and degradation and they exert their function in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregration and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (3). Recent data has demonstrated that BAG-1 which possesses a ubiquitin-like domain at its amino terminus and has been shown to associate with the 26S proteosome in HeLa cells, modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal a role of BAG-1 as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome (4). There is also experimental data which shows that the ATPase domain and the substrate binding domain of Hsp70 (or Hsc70) cooperate and form a cochaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp) which is essential for normal neurotransmitter release (5).

Applications:
Suitable for use in Western Blot and Immunohistochemistry. Other applications have not been tested.

Recommended Dilutions:
Western Blot (Colorimetric): 1:1000
Immunohistochemistry: paraffin
Optimal dilutions to be determined by researcher.

Positive Controls:
Recombinant Human Hsp70 Protein, Heat Shocked HeLa Cell Lysate, Recombinant Hsc70 Protein

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.

Applications
Product Type: Pab|Isotype: IgG|Host: rabbit|Source: rat|Concentration: ~1mg/ml|Form: Supplied as a liquid in PBS, 0.09% sodium azide, 50% glycerol.|Purity: Purified by Protein A affinity chromatography.|Immunogen: Synthetic peptide corresponding to the sequence of rat Hsp70|Specificity: Recognizes rat Hsp70 at ~72 and 73kD. Species Crossreactivity: human, monkey, mouse, sheep, bovine, rabbit, porcine, hamster, canine, chicken, guinea pig, Drosophila, plant, yeast and fish. ||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Immunogen
Synthetic peptide corresponding to the sequence of rat Hsp70
Form
Supplied as a liquid in PBS, 0.09% sodium azide, 50% glycerol.
Purity
Purified by Protein A affinity chromatography.
Specificity
Recognizes rat Hsp70 at ~72 and 73kD. Species Crossreactivity: human, monkey, mouse, sheep, bovine, rabbit, porcine, hamster, canine, chicken, guinea pig, Drosophila, plant, yeast and fish.
References
1. Kurucz, I., Tombor, B., Prechl, J., Erdo, F., Hegedus, E., Nagy, Z., Vitai, M., Koranyi, L. and Laszlo, L. (1999) Cell Stress & Chaperones 4:139-152. 2. Tavaria, M., Gabriele, T., Kola, I. and Anderson, RL. (1996) Cell Stress & Chaperones 1:23-28. 3. Fink AL. (1999) Physiol Rev 79:425-49. 4. Luders, J., Demand, J. and Hohfeld, J. (2000) J Biol Chem 275:4613-7. 5. Stahl B., Tobaben, S. and Sudhof, TC. (1999) Eur. J. Cell Biol 78:375-81.