HSP70 Protein (Heat Shock Protein 70) (His tag)
- Target Alle HSP70 Proteine anzeigen
- HSP70 (Heat Shock Protein 70 (HSP70))
- Biologische Aktivität
- Baculovirus infected Insect Cells
- Aufreinigungstag / Konjugat
- Dieses HSP70 Protein ist gelabelt mit His tag.
- Activity Assay (AcA), ELISA, Functional Studies (Func), SDS-PAGE (SDS), Western Blotting (WB)
- MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
- ~70 kDa
- The protein tested positive for ATPase activity using a Malachite Green assay.
- Affinity Purified | Endotoxin-free
- Biological Activity Comment
- ATPase active
- Optimal working dilution should be determined by the investigator.
This product has been certified >90% pure using SDS-PAGE analysis. The protein tested positive for ATPase activity using a Malachite Green assay.
- Nur für Forschungszwecke einsetzbar
- Lot specific
- 20 mM Tris, 150 mM NaCl, 10 % glycerol
- -20 °C
The heat shock response in congeneric land snails (Sphincterochila) from different habitats." in: Cell stress & chaperones, Vol. 17, Issue 5, pp. 639-45, (2012) (PubMed).
: "Heat shock proteins and resistance to desiccation in congeneric land snails." in: Cell stress & chaperones, Vol. 15, Issue 4, pp. 351-63, (2010) (PubMed).
- The heat shock response in congeneric land snails (Sphincterochila) from different habitats." in: Cell stress & chaperones, Vol. 17, Issue 5, pp. 639-45, (2012) (PubMed).
- HSP70 (Heat Shock Protein 70 (HSP70))
- Andere Bezeichnung
- Hsp70 (HSP70 Produkte)
- APG-2, HS24/P52, HSPH2, RY, hsp70, hsp70RY, CG31354, HSP70, Hsp70Bb, hsp70B, hsp70Bb-prime, DmelCG5834, CG5834, HSPA1, HSP70B', HSPA6, ARABIDOPSIS HEAT SHOCK PROTEIN 70, ATHSP70, heat shock protein 70, LOC100305036, hsc70, Hsp70, Hsp70-1, Hsp70.1, hsp68, Hsp110, irp94, HSP70-2, HSPA1B, HSPA2, hsp70-5, HSP70-1, HSP70.1, HSP70.2, heat shock protein family A (Hsp70) member 4, CG5834 gene product from transcript CG5834-RA, heat shock protein 70, heat shock protein family A (Hsp70) member 6, heat shock 70kDa protein 2, heat shock 70 kD protein cognate, Hsp70 family chaperone, Heat shock protein 70, Heat shock protein 70, putative, heat shock protein 1B, heat shock protein family A member 4, heat shock 70kDa protein 1A, heat shock protein 1, Heat Shock Protein, heat shock cognate 70-kd protein, Heat shock 70 kDa protein 1A, HSPA4, Hsp70Bbb, HSP70, HSPA6, HSPA2, PCC7424_2419, Isop_1041, CGB_C3390W, Bacsa_1698, dnaK-B, LOC100305036, Hspa1b, Hspa4, HSPA1A, hsp1, hsp-70, hsp70, LOC108348108
- 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 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 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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.
- approx. 70 kDa
- NCBI Accession