Human Heat Shock Protein 27 ELISA Kit (HSP27) (ab108862)
Key features and details
- Sensitivity: 0.16 ng/ml
- Range: 1.25 ng/ml - 20 ng/ml
- Sample type: Cell Lysate, Milk, Plasma, Serum, Tissue
- Detection method: Colorimetric
- Assay type: Sandwich (quantitative)
- Reacts with: Human
Overview
-
Product name
Human Heat Shock Protein 27 ELISA Kit (HSP27)
See all Heat Shock Protein 27 (HSP27) kits -
Detection method
Colorimetric -
Precision
Intra-assay Sample n Mean SD CV% Overall 4.8% Inter-assay Sample n Mean SD CV% Overall 9.9% -
Sample type
Milk, Serum, Plasma, Tissue, Cell Lysate -
Assay type
Sandwich (quantitative) -
Sensitivity
> 0.16 ng/ml -
Range
1.25 ng/ml - 20 ng/ml -
Recovery
97 %
-
Assay time
5h 00m -
Assay duration
Multiple steps standard assay -
Species reactivity
Reacts with: Human -
Product overview
Abcam’s Heat Shock Protein 27 (HSP27) Human in vitro ELISA (Enzyme-Linked Immunosorbent Assay) kit is designed for the quantitative measurement of HSP27 levels in cell culture samples, milk, serum, plasma and tissue extract.
A HSP27 specific antibody has been precoated onto 96-well plates and blocked. Standards or test samples are added to the wells and subsequently a HSP27 specific biotinylated detection antibody is added and then followed by washing with wash buffer. Streptavidin-Peroxidase Conjugate is added and unbound conjugates are washed away with wash buffer. TMB is then used to visualize Streptavidin-Peroxidase enzymatic reaction. TMB is catalyzed by Streptavidin-Peroxidase to produce a blue color product that changes into yellow after adding acidic stop solution. The density of yellow coloration is directly proportional to the amount of HSP27 captured in plate.
Get results in 90 minutes with Human Heat Shock Protein 27 ELISA Kit (HSP27) (ab193757) from our SimpleStep ELISA® range.
The entire kit may be stored at -20°C for long term storage before reconstitution - Avoid repeated freeze-thaw cycles.
-
Platform
Microplate
Properties
-
Storage instructions
Store at -20°C. Please refer to protocols. -
Components 1 x 96 tests 100X Streptavidin-Peroxidase Conjugate 1 x 80µl 10X Diluent M Concentrate 1 x 20ml 1X Standard Diluent 1 x 2ml 20X Wash Buffer Concentrate 2 x 30ml 50X Biotinylated Human HSP27 Antibody 1 x 120µl Chromogen Substrate 1 x 7ml HSP27 Microplate (12 x 8 well strips) 1 unit HSP27 Standard 1 vial Sealing Tapes 3 units Stop Solution 1 x 11ml -
Research areas
-
Relevance
Involved in stress resistance and actin organization. Interacts with TGFB1I1. Associates with alpha- and beta-tubulin, microtubules and CRYAB. Interacts with HSPB8 and HSPBAP1. -
Cellular localization
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. -
Alternative names
- HSPB1
- 28 kDa heat shock protein
- CMT2F
see all -
Database links
- Entrez Gene: 3315 Human
- Omim: 602195 Human
- SwissProt: P04792 Human
Datasheets and documents
-
SDS download
-
Datasheet download
References (5)
ab108862 has been referenced in 5 publications.
- Zhou XY et al. TAT-HSP27 Peptide Improves Neurologic Deficits via Reducing Apoptosis After Experimental Subarachnoid Hemorrhage. Front Cell Neurosci 16:878673 (2022). PubMed: 35573833
- White NM et al. Quantitative proteomic analysis reveals potential diagnostic markers and pathways involved in pathogenesis of renal cell carcinoma. Oncotarget 5:506-18 (2014). PubMed: 24504108
- Enomoto M et al. Newborn rat response to single vs. combined cGMP-dependent pulmonary vasodilators. Am J Physiol Lung Cell Mol Physiol 306:L207-15 (2014). WB . PubMed: 24242011
- Jin C et al. Plasma heat shock protein 27 is associated with coronary artery disease, abdominal aortic aneurysm and peripheral artery disease. Springerplus 3:635 (2014). PubMed: 25392804
- Thanabalasundaram G et al. Cortical non-aneurysmal subarachnoid hemorrhage post-carotid endarterectomy: a case report and literature review. Springerplus 2:571 (2013). PubMed: 24255864