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HSP27 Antibody (Center)Purified Rabbit Polyclonal Antibody (Pab)

Country
United States
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Ordering Information
Catalog # Size Availability Price  
AP7199e 400 µl (40 western blots) In Stock $ 265.00 Add to cart
AP7199e-ev 80 µl (8 western blots) In Stock $ 95.00 Add to cart
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HSP27 Antibody (Center) - Product info

ApplicationWB, IHC
  • Applications Legend:
  • WB=Western Blotting
  • IP=Immunoprecipitation
  • IHC-P=Immunohistochemistry (Paraffin)
  • IF-IC=Immunofluorescence (Immunocytochemistry)
  • FC=Flow Cytometry
  • DB=Dot Blot
Primary AccessionP04792
Other AccessionP42930, P14602, Q3T149
ReactivityHuman
PredictedMouse, Rat, Bovine
IsotypeRabbit Ig
Calculated MW22783 Da

HSP27 Antibody (Center) - Additional info

Gene ID 3315
Other Names
HSPB1; HSP27; HSP28; Heat shock protein beta-1; 28 kDa heat shock protein; Estrogen-regulated 24 kDa protein; Heat shock 27 kDa protein; Stress-responsive protein 27
Target/Specificity
This HSP27 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 108-136 amino acids from the Central region of human HSP27.
Dilution
WB~~1:1000
IHC~~1:50~100
Format
Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Storage
Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
Precautions
HSP27 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.

HSP27 Antibody (Center) - Protein Information

Name HSPB1
Synonyms HSP27, HSP28
Function
Involved in stress resistance and actin organization.
Cellular Location
Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles
Tissue Location
Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle

HSP27 Antibody (Center) - Related products

AP3347a: Phospho-HSPB1(S78) Antibody

AP7199a: HSP27 (HSPB1) Antibody (S83)

AP7199c: HSP27 (HSPB1) Antibody (S78)

AP7199d: HSPB1 Antibody (S82)

BP3347a: Phospho-HSPB1-S78 Antibody Blocking Peptide

BP7199a: HSPB1 Antibody (S83) Blocking Peptide

BP7199b: HSPB1 Antibody (S15) Blocking Peptide

BP7199c: HSPB1 Antibody (S78) Blocking Peptide

BP7199d: HSPB1 Antibody (S82) Blocking Peptide

BP7199e: HSP27 Antibody (Center) Blocking Peptide

AJ1378a: HSP27 Antibody

AJ1378b: HSP27 Antibody Phospho (pS15)

AJ1378c: HSP27 Antibody Phospho (pS78)

HSP27 Antibody (Center) - Application data

  • Western blot analysis of HSP27 antibody (Center) (Cat.# AP7199e) in MCF-7 cell line lysates (35ug/lane). HSP27 (arrow) was detected using the purified Pab.

  • Hsp 27 Antibody (Center) (Cat.# AP7199e) IHC analysis in formalin fixed and paraffin embedded human Lung carcinoma followed by peroxidase conjugation of the secondary antibody and DAB staining. This data demonstrates the use of the Hsp 27 Antibody (Center) for immunohistochemistry. Clinical relevance has not been evaluated.

HSP27 Antibody (Center) - Research Areas

AntibodiesGene OntologyBiological ProcessCell DeathCellular ProcessRegulation Of Cell DeathRegulation Of Programmed Cell DeathResponse To Organic SubstanceRegulation Of ApoptosisNegative Regulation Of Cellular ProcessNegative Regulation Of Biological ProcessResponse To Chemical StimulusNegative Regulation Of ApoptosisNegative Regulation Of Cell DeathRegulation Of Protein Metabolic ProcessNegative Regulation Of Programmed Cell DeathRegulation Of Cellular Protein Metabolic ProcessResponse To StressDeathAnti-apoptosisRegulation Of Metabolic ProcessRegulation Of Cellular Metabolic ProcessCell MotionBiological RegulationRegulation Of Macromolecule Metabolic ProcessResponse To Protein StimulusResponse To Abiotic StimulusRegulation Of Primary Metabolic ProcessRegulation Of Biological ProcessResponse To Unfolded ProteinResponse To StimulusRegulation Of Cellular ProcessPosttranscriptional Regulation Of Gene ExpressionResponse To Temperature StimulusResponse To Biotic StimulusResponse To HeatCellular CompartmentCell SurfaceCytoplasmNucleusIntracellular PartIntracellularCytoplasmic PartMembrane-bounded OrganelleIntracellular Membrane-bounded OrganelleOrganelleIntracellular OrganelleOrganelle PartIntracellular Organelle PartSoluble FractionInsoluble FractionMacromolecular ComplexProtein ComplexMolecular FunctionProtein BindingIdentical Protein BindingPathwaysBiocartaP38 MAPK Signaling Pathway KEGGMAPK Signaling PathwayVEGF Signaling PathwayPantherP38 MAPK PathwayTissueBrianLungOvaryPancreasSkinUterusPlateletEpitheliumMammary CarcinomaCervix CarcinomaEmbryonic KidneyHepatocyte

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BACKGROUND

In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. HSBP1 exhibits rapid increased phosphorylation in response to various mitogens, tumor promoters (e.g. phorbol esters) and calcium ionophores, and high levels are associated with carcinoma of the breast and with endometrial adenocarcinomas. Heat shock of HeLa cell cultures, or treatment with arsenite, phorbol ester, or tumor necrosis factor, causes a rapid phosphorylation of preexisting HSBP1, with Ser82 as the major site and Ser78 the minor site of phosphorylation. HSBP1 may exert phosphorylation-activated functions linked with growth signaling pathways in unstressed cells. A homeostatic function at this level could protect cells from adverse effects of signal transduction systems which may be activated inappropriately during stress.

REFERENCES

Wano, C., et al., Exp. Cell Res. 298(2):584-592 (2004).
Evgrafov, O.V., et al., Nat. Genet. 36(6):602-606 (2004).
Song, H., et al., Biochem. Biophys. Res. Commun. 314(1):143-150 (2004).
Chauhan, D., et al., Blood 102(9):3379-3386 (2003).
Van Why, S.K., et al., J. Am. Soc. Nephrol. 14(1):98-106 (2003).