Analytical Data
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Gene name
HSP47
- Application
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Alternative Names
SERPINH1;CBP1;CBP2;HSP47;Serpin H1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
19-418aa
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AA Sequence
AEVKKPAAAAAPGTAEKLSPKAATLAERSAGLAFSLYQAMAKDQAVENIL VSPVVVASSLGLVSLGGKATTASQAKAVLSAEQLRDEEVHAGLGELLRSL SNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRS ALQSINEWAAQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKM VDNRGFMVTRSYTVGVMMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLI ILMPHHVEPLERLEKLLTKEQLKIWMGKMQKKAVAISLPKGVVEVTHDLQ KHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFELDTDGNPFDQ DIYGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRPKGDKMRDEL
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Molecular Weight
46 kDa
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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 the folding and assembly of collagen molecules, which are essential for the structural integrity of tissues. Research has increasingly focused on HSP47 due to its significant involvement in various pathological conditions, including fibrosis, cancer, and certain genetic disorders related to collagen synthesis. Since HSP47 is associated with the endoplasmic reticulum and the intracellular transport of collagen, it serves as a vital player in extracellular matrix (ECM) homeostasis. Recombinant HSP47 protein has gained attention for its potential therapeutic applications, including the development of antifibrotic agents and strategies to enhance collagen-based tissue engineering. By producing HSP47 in a recombinant form, researchers are able to explore its structure-function relationships, to investigate its role in modulating cellular responses, and to evaluate its efficacy in inhibiting collagen-related diseases. This research can provide insights into the molecular mechanisms underlying collagen disorders and facilitate the design of novel therapeutic interventions aimed at regulating ECM dynamics in various clinical settings. As such, the study of recombinant HSP47 protein not only aids in understanding fundamental biological processes but also holds promise for advancing treatment options for collagen-related pathologies.
