Human HSP27 Antibody

Catalog # Availability Size / Price Qty
AF1580
AF1580-SP
Detection of Human HSP27 by Western Blot.
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Product Details
Citations (6)
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Human HSP27 Antibody Summary

Species Reactivity
Human
Specificity
Detects recombinant and endogenous human HSP27 in Western blots.
Source
Polyclonal Rabbit IgG
Purification
Antigen Affinity-purified
Immunogen
E. coli-derived recombinant human HSP27
Accession # P04792
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. See Certificate of Analysis for details.
*Small pack size (-SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Label
Unconjugated

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
HeLa human cervical epithelial carcinoma cell line and DU145 human prostate carcinoma cell line
Simple Western
0.5 µg/mL
HeLa human cervical epithelial carcinoma cell line
Knockout Validated
HSP27 is specifically detected in HeLa humancervical epithelial carcinoma parental cell line but is not detectable inHSP27 knockout HeLa cell line.
 

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Western Blot View Larger

Detection of Human HSP27 by Western Blot. Western Blot shows lysates of HeLa human cervical epithelial carcinoma cell line and DU145 human prostate carcinoma cell line. PVDF membrane was probed with 0.1 µg/ml of Rabbit Anti-Human HSP27 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1580) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for HSP27 at approximately 27 kDa (as indicated). This experiment was conducted under reducing conditions and using Western Blot Buffer Group 1.

Simple Western Detection of Human HSP27 antibody by Simple Western<SUP>TM</SUP>. View Larger

Detection of Human HSP27 by Simple WesternTM. Simple Western lane view shows lysates of HeLa human cervical epithelial carcinoma cell line, loaded at 0.2 mg/mL. A specific band was detected for HSP27 at approximately 31 kDa (as indicated) using 0.5 µg/mL of Rabbit Anti-Human HSP27 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1580). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.

Knockout Validated Western Blot Shows Human HSP27 Antibody Specificity by Using Knockout Cell Line. View Larger

Western Blot Shows Human HSP27 Specificity by Using Knockout Cell Line. Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and HSP27 knockout HeLa cell line (KO). PVDF membrane was probed with 0.5 µg/mL of Rabbit Anti-Human HSP27 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1580) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (HAF008). A specific band was detected for HSP27 at approximately 27 kDa (as indicated) in the parental HeLa cell line, but is not detectable in knockout HeLa cell line. GAPDH (MAB5718) is shown as a loading control. This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.

Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration.
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Shipping
Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Background: HSP27

Heat shock proteins (HSPs) are a family of highly conserved stress response proteins. Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways. HSPs are typically expressed at low levels under normal physiological conditions but are dramatically up-regulated in response to cellular stress. Elevated levels of HSPs have been observed in association with ischemia/reperfusion, cancer, and chronic heart failure. HSP27, also known as HSPB1, is a member of the small heat shock protein family, which also includes HSP25 and the alpha -crystallins. HSP27 forms a large oligomer and the extent of phosphorylation plays a role in determining specific functions. HSP27 also functions as an anti-apoptotic molecule, regulating apoptosis through direct interaction with key components of the apoptotic pathway. HSP27 binds and sequesters cytochrome c released from the mitochondria in response to an apoptotic stimulus. This prevents the proper assembly of the apoptosome and subsequently, the activation of procaspase-9 and procaspase-3. Full length human HSP27 shares 83% and 81% aa identity with mouse and rat HSP27, respectively.

References
  1. Gusev, N.B. et al. (2002) Biochemistry (Moscow) 67:511.
  2. Garrido, C. et al. (2001) Biochem. Biophys. Res. Commun. 286:433.
  3. Garrido, C. (2002) Cell Death Diffr. 9:483.
  4. Brvey, J-M. et al. (2000) Nat. Cell Biol. 2:645.
Long Name
Heat Shock Protein 27
Entrez Gene IDs
3315 (Human); 15510 (Mouse); 24471 (Rat)
Alternate Names
28 kDa heat shock protein; DKFZp586P1322; Estrogen-regulated 24 kDa protein; Heat shock 27 kDa protein; heat shock 27kD protein 1; heat shock 27kDa protein 1; heat shock protein beta-1; HMN2B; HS.76067; HSP25; HSP27; HSP27HSP 27; HSP28CMT2F; HSPB1; SRP27; Stress-responsive protein 27

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Citations for Human HSP27 Antibody

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

6 Citations: Showing 1 - 6
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  1. Divergent single cell transcriptome and epigenome alterations in ALS and FTD patients with C9orf72 mutation
    Authors: Li J, Jaiswal MK, Chien JF et al.
    Nat Commun
    Applications: Simple Western
  2. Einfluss der Phosphorylierung des Hitzeschockproteins 27 auf das Expressionsprofil von parodontalen Ligamentfibroblasten bei mechanischer Belastung
    Authors: Agnes Schröder, Kathrin Wagner, Fabian Cieplik, Gerrit Spanier, Peter Proff, Christian Kirschneck
    Journal of Orofacial Orthopedics / Fortschritte der Kieferorthopädie
  3. Increased expression of phosphorylated forms of heat-shock protein-27 and p38MAPK in macrophage-rich regions of fibro-fatty atherosclerotic lesions in the rabbit
    Authors: Shahida Shafi, Rosalind Codrington, Lewis Michael Gidden, Gordon Ashley Anthony Ferns
    International Journal of Experimental Pathology
  4. Heat shock protein 27 differentiates tolerogenic macrophages that may support human breast cancer progression.
    Authors: Banerjee S, Lin CF, Skinner KA, Schiffhauer LM, Peacock J, Hicks DG, Redmond EM, Morrow D, Huston A, Shayne M, Langstein HN, Miller-Graziano CL, Strickland J, O'Donoghue L, De AK
    Cancer Res., 2011-01-11;71(2):318-27.
    Species: Human
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  5. The heat shock response and chaperones/heat shock proteins in brain tumors: surface expression, release, and possible immune consequences.
    Authors: Graner MW, Cumming RI, Bigner DD
    J. Neurosci., 2007-10-17;27(42):11214-27.
    Species: Human
    Sample Types: Cell Lysates
    Applications: Western Blot
  6. Phosphatidylinositol 3-kinase/Akt plays a role in sphingosine 1-phosphate-stimulated HSP27 induction in osteoblasts.
    Authors: Takai S, Tokuda H, Matsushima-Nishiwaki R, Hanai Y, Kato K, Kozawa O
    J. Cell. Biochem., 2006-08-01;98(5):1249-56.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Western Blot

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