Description
Key facts
Detection method:Colorimetric,
Sample types:Cell culture extracts, Citrate plasma, Serum, Cell Lysate,
Reacts with:Mouse, Rat, Human,
Assay type:Sandwich (quantitative),
Sensitivity:= 119.23 pg/mL,
Range:218.75 - 14000 pg/mL,
Assay time:1h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)
Product details:
HSP47 ELISA kit (ab270882) is a single-wash 90 min sandwich ELISA designed for the quantitative measurement of HSP47 protein in human serum and plasma (citrate) and human, mouse and rat cell and tissue extract samples. It uses our proprietary SimpleStep ELISA® technology. Quantitate HSP47 with 119.23 pg/mL sensitivity.
SimpleStep ELISA® technology employs capture antibodies conjugated to an affinity tag that is recognized by the monoclonal antibody used to coat our SimpleStep ELISA® plates. This approach to sandwich ELISA allows the formation of the antibody-analyte sandwich complex in a single step, significantly reducing assay time. See the SimpleStep ELISA® protocol summary in the image section for further details. Our SimpleStep ELISA® technology provides several benefits:
-Single-wash protocol reduces assay time to 90 minutes or less
-High sensitivity, specificity and reproducibility from superior antibodies
-Fully validated in biological samples
-96-wells plate breakable into 12 x 8 wells strips
A 384-well SimpleStep ELISA® microplate (ab203359) is available to use as an alternative to the 96-well microplate provided with SimpeStep ELISA® kits.
Heat Shock Protein47 (HSP47) is a collagen specific molecular chaperone protein found in the endoplasmic reticulum. HSP47 assists in the triple-helical formation of collagen and is part of the collagen quality control system. Collagen accounts for approximately 30% of the total protein found in vertebrates and is the major component responsible in providing structural support for a number of tissues. HSP47 can be found constitutively expressed in non-stressed cells associated with collagen expression. Increased HSP47 expression has been associated with increase collagen deposition in arteriosclerosis, myocardial infarction, hepatic fibrosis, renal fibrosis, and pulmonary fibrosis.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-+4°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Hsp47 also known as the heat shock protein 47 is a molecular chaperone with a molecular weight of approximately 47 kDa. It mainly resides in the endoplasmic reticulum and participates in collagen synthesis. Hsp47 binds specifically to unfolded procollagen chains ensures their proper folding and prevents premature aggregation. Due to its specialized function Hsp47 is highly expressed in collagen-producing cells like fibroblasts. Researchers commonly study this protein using techniques like Hsp47 ELISA to measure its expression or activity levels.
Biological function summary
Hsp47 ensures the quality control of collagen within the secretory pathway. It does not form part of any large protein complexes but operates closely with collagen molecules. By stabilizing procollagen's triple-helix structure Hsp47 plays an important role in collagen biosynthesis. Dysfunctional collagen processes can arise without this protein's presence potentially leading to cellular stress or structural weaknesses within tissues rich in collagen.
Pathways
Hsp47's activity integrates into the collagen synthesis and secretion pathways. This protein is related to other molecular chaperones such as Hsp70 that assist in maintaining protein homeostasis within the cell. Hsp47’s function links to fibrosis pathways because of its role in collagen maturation. In terms of fibrotic pathologies this involvement makes the chaperoning of procollagen a critical control point.
Disrupted Hsp47 function frequently associates with fibrotic conditions and osteogenesis imperfecta. Fibrosis results from excessive collagen deposition in which Hsp47 is deeply implicated. Additionally certain cancer types have shown altered Hsp47 expression correlating with increased cancer cell invasiveness due to extracellular matrix remodeling. Studies have noted interactions between Hsp47 and TGF-beta signaling in fibrotic tissues reinforcing its role in pathological collagen turnover.
