Analytical Data
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Gene name
HSP47
- Application
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Alternative Names
CBP2; AsTP3; CBP1; PIG14; RA-A47; SERPINH1; SERPINH2; Colligen; Gp46; Serpin Peptidase Inhibitor Clade H Member 1; Heat Shock Protein 47; Collagen Binding Protein 2
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P50454
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Expression Region
Pro30~Leu418
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Molecular Weight
47kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
HSP47, or Heat Shock Protein 47, is a collagen-specific molecular chaperone that plays a crucial role in collagen biosynthesis and folding in the endoplasmic reticulum (ER). It is essential for the proper assembly and secretion of collagen, which is a major component of the extracellular matrix and vital for tissue integrity and repair. Research on HSP47 has significantly increased due to its implications in various pathological conditions, including fibrosis, where abnormal collagen accumulation leads to tissue scarring and dysfunction, and cancer, where altered collagen metabolism can influence tumor progression and metastasis. Moreover, HSP47 has been identified as a potential therapeutic target and biomarker for fibrotic diseases and cancer. The recombinant expression of HSP47 enables the study of its structure-function relationships, interaction with collagen substrates, and its role in chaperoning processes. Scientists utilize recombinant HSP47 in various experimental models to unravel its mechanisms in collagen-related diseases and to explore therapeutic interventions aimed at modulating its activity. The development of HSP47-based treatments holds promise for managing disorders characterized by collagen dysregulation and offers insights into the broader implications of protein folding diseases.
