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HSP70/HSC70 (Plant) Antibody: Dylight 488, Monoclonal

HSP70/HSC70 (Plant) Antibody: Dylight 488, Monoclonal
331,97 €
Artikelnummer: STRSMC-120D-DY488

Verfügbarkeit: Regellieferzeit: Innerhalb 1 - 2 Wochen

Kostenlose Lieferung innerhalb Österreichs!
HSP70/HSC70 (Plant) Antibody: Dylight 488, Monoclonal, Clone: 5G1-95, Host: Mouse, Isotype: IgG1


Mouse Anti-Plant HSP70/HSC70 Monoclonal IgG1
Target: HSP70/HSC70
Purification: Protein G Purified
Specificity: Detects ~70kDa. Recognizes constitutive and inducible plants HSP70 (HSC70/HSP72). Does not cross-react with Human, Rat, bacteria (DNAK) or Human Bip.
Conjugate: Dylight 488
Immunogen Species: Plant
Cellular Location: Cytoplasm
Immunogen: Purified HSP70 from Phaseolus aureus (mung bean)
Scientific 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.
Reference: 1. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol.38 (1): 1-17.2. Rothman J. (1989) Cell 59: 591-601.3. DeLuca-Flaherty et al. (1990), Cell 62: 875-887.4. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294.5. Fink A.L. (1999) Physiol. Rev. 79: 425-449.


Artikelnummer STRSMC-120D-DY488
Hersteller Stressmarq Biosciences
Herstellernummer SMC-120D-DY488
Verpackungseinheit 100 µg
Mengeneinheit FL
Reaktivität Plant
Klonalität Monoclonal
Wirt / Host Mouse
Methode ELISA, Western Blotting
Isotype IgG1
Gene ID Keine Herstellerangabe
Datenblatt Download
MSDS Download