Heat Shock 27kDa Protein 1 (HSPB1) (full length) Protéine

Détails pour le produit réf. ABIN1686697
Nom de la protéine
  • CMT2F
  • HMN2B
  • HS.76067
  • HSP27
  • HSP28
  • Hsp25
  • SRP27
  • 27kDa
  • Hsp27
  • cb153
  • cb660
  • hsp1
  • hsp25
  • hsp27
  • id:ibd2821
  • sb:cb660
  • zgc:103437
  • HSPB1
  • cmt2f
  • hs.76067
  • hsp28
  • heat shock protein family B (small) member 1
  • heat shock protein 1
  • heat shock protein, alpha-crystallin-related, 1
  • heat shock protein family B (small) member 1 L homeolog
  • HSPB1
  • Hspb1
  • hspb1
  • hspb1.L
Attributs du protein
full length
4
3
2
1
1
1
1
1
1
Origine
Humain
19
3
2
2
1
1
1
Source
Escherichia coli (E. coli)
19
5
2
2
1
Type de proteíne
Recombinant
Application
ELISA, Functional Studies (Func), SDS-PAGE (SDS), Western Blotting (WB)
Options
Séquence MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD ETAAK
Specificité ~27 kDa
Purification Affinity Purified
Pureté >90%
Nom de la protéine
Sujet HSP27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic structure of most sHSPs is a homologous and highly conserved amino acid sequence, with an α-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (1, 2). HSP27-oligomers consist of stable dimers formed by as many as 8-40 HSP27 protein monomers (3). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (4). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. Other functions include chaperone activity (as mentioned above), thermo tolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. HSP27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that HSP27 may serve some role in cross-bridge formation between actin and myosin (5). And finally, HSP27 is also thought to be involved in the process of cell differentiation. The up-regulation of HSP27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that HSP27 may play a crucial role in termination of growth (6). Looking for more information on HSP27? Visit our new HSP27 Scientific Resource Guide at http://www.HSP27.com.
Poids moléculaire approx. 27 kDa
ID gène 3315
UniProt P04792
Pathways Signalisation MAPK, Regulation of Actin Filament Polymerization, Signaling Events mediated by VEGFR1 and VEGFR2, Negative Regulation of intrinsic apoptotic Signaling, VEGF Signaling
Commentaires

This product has been certified >90% pure using SDS-PAGE analysis.

Restrictions For Research Use only
Concentration Lot specific
Buffer 20 mM Tris/HCl pH 7.5, 0.45M NaCl, 10 % glycerol, 5 mM DTT
Stock -20 °C
Background publications Van Montfort, Slingsby, Vierling: "Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones." dans: Advances in protein chemistry, Vol. 59, pp. 105-56, 2002 (PubMed).

Ehrnsperger, Gräber, Gaestel, Buchner: "Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation." dans: The EMBO journal, Vol. 16, Issue 2, pp. 221-9, 1997 (PubMed).

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