/ Stressmarq Product-Datasheet SPC-103D

Biomol GmbH
Waidmannstr. 35
22769 HAMBURG
info@biomol.de
www.biomol.de
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0800 - 24 66 652 free call

Product Name
Hsp70 Antibody
Catalog #
SPC-103D
Package size
100ul
 
Bulk Quote
Alternate Product Sizes
SPC-103C
Type
Polyclonal
Datasheet
SPC 103 Heat Shock Protein 70 (Hsp70)
Description
Anti-Hsp70
Research Area
Chaperones, Heat Shock, Trafficking
Alternative Names
Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B
Clone Number
N/A
Host Species
Rabbit
Isotype
N/A
Immunogen
Full length human protein Hsp70
Applications
WB, IP, ELISA, IHC, ICC, IF
Species Reactivity
Human, Mouse, Rat, Beluga, Cow, Dog, Fish (carp), Guinea Pig, Hamster, Monkey, Pig, Sheep, Coral, Tomato, Tobacco, Spiny dogfish shark (Squalus acanthias), Atlantic Hagfish (Myxine glutinosa), Rainbow Trout
Accession Number
NP_005336.3
Gene ID
3303
SwissProt
P08107
Background Info
Detects a ~70kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS PAGE immunoblots. May cross-react with Hsc70 at lower dilutions.
Recommended Dilutions
1:25,000 (ECL) (WB), 1:100 (IP)
Form
Rabbit antiserum
Storage Buffer
Rabbit antiserum
Concentration
N/A
Certificate of Analysis
A 1:10,000 dilution of SPC-103 was sufficient for detection of hsp70 in 20μg of HeLa cell lysate by ECL immunoblot analysis.
Storage Temp
-20°C
Shipping Temp
Blue Ice or 4°C

This antibody is available conjugated to several dyes. Please select one of the conjugates from the lists below:

ATTO Conjugates:

ATTO-Conjugates.pdf

Enzyme & Fluorescent Conjugates:

Enzyme-Fluorescent-Conjugate.pdf
hsp70 antibody Western blot analysis of Hsp70 in Pam212 cells using a 1:1000 dilution of SPC-103. Western blot analysis of Hsp70 in multiple human and rat brain cell lysates using a 1:1000 dilution of SPC-103. Hsp70 visualized using SPC-103, tested on Bouin's fixed paraffin-embedded backskin sections of transgenic mice. Courtesy of Dr. Turksen, Ottawa  Hospital Research Institute, Canada.
Research 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 5O% identity (1, 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 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 ATPbinding 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.
References
1. Welch W.J. and Suhan J.P. (1986) J.Cell Biol. 103: 2035-2050. 2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol. 38(1): 1-17. 3. Rothman J. (1989) Cell 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Hung T.H., et al. (2001) Am J Pathol. 159: 1031-1043. 8. Locke M. (2000) Cell Stress & Chaperones 5: 45-51. 9. Ianaro A., et al. (2001) FEBS Lett. 508: 61-66. 10.Trentin G.A. et al. (2001) J Biol Chem. 276: 13087- 13095.


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