HSP27 Protein (full length)

Catalog No. ABIN1686697

Product Details

Target: HSP27 (HSPB1) (Heat Shock 27kDa Protein 1 (HSPB1))

Protein Type: Recombinant

Protein Characteristics: full length

Origin: Human

Source: Escherichia coli (E. coli)

Application: Western Blotting (WB), ELISA, SDS-PAGE (SDS), Functional Studies (Func)

Sequence: MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD ETAAK

Specificity: ~27 kDa

Purification: Affinity Purified

Purity: >90%

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

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

Restrictions: For Research Use only

Handling

Concentration: Lot specific

Buffer: 20 mM Tris/HCl pH 7.5, 0.45M NaCl, 10 % glycerol, 5 mM DTT

Storage: -20 °C

Target Details

Target: HSP27 (HSPB1) (Heat Shock 27kDa Protein 1 (HSPB1))

Alternative Name: Hsp27 (HSPB1 Products)

Synonyms: CMT2F Protein, HMN2B Protein, HS.76067 Protein, HSP27 Protein, HSP28 Protein, Hsp25 Protein, SRP27 Protein, 27kDa Protein, Hsp27 Protein, cb153 Protein, cb660 Protein, hsp1 Protein, hsp25 Protein, hsp27 Protein, id:ibd2821 Protein, sb:cb660 Protein, zgc:103437 Protein, HSPB1 Protein, cmt2f Protein, hs.76067 Protein, hsp28 Protein, heat shock protein family B (small) member 1 Protein, heat shock protein 1 Protein, heat shock protein, alpha-crystallin-related, 1 Protein, heat shock protein family B (small) member 1 L homeolog Protein, HSPB1 Protein, Hspb1 Protein, hspb1 Protein, hspb1.L Protein

Background: 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.

Molecular Weight: approx. 27 kDa

Gene ID: 3315

UniProt: P04792

Pathways: MAPK Signaling, Regulation of Actin Filament Polymerization, Signaling Events mediated by VEGFR1 and VEGFR2, Negative Regulation of intrinsic apoptotic Signaling, VEGF Signaling