Analytical Data
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基因名
HSP47
- Application
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别名
SERPINH1;CBP1;CBP2;HSP47;Serpin H1
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P50454
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表达区间
19-418aa
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氨基酸序列
AEVKKPAAAAAPGTAEKLSPKAATLAERSAGLAFSLYQAMAKDQAVENIL VSPVVVASSLGLVSLGGKATTASQAKAVLSAEQLRDEEVHAGLGELLRSL SNSTARNVTWKLGSRLYGPSSVSFADDFVRSSKQHYNCEHSKINFRDKRS ALQSINEWAAQTTDGKLPEVTKDVERTDGALLVNAMFFKPHWDEKFHHKM VDNRGFMVTRSYTVGVMMMHRTGLYNYYDDEKEKLQIVEMPLAHKLSSLI ILMPHHVEPLERLEKLLTKEQLKIWMGKMQKKAVAISLPKGVVEVTHDLQ KHLAGLGLTEAIDKNKADLSRMSGKKDLYLASVFHATAFELDTDGNPFDQ DIYGREELRSPKLFYADHPFIFLVRDTQSGSLLFIGRLVRPKGDKMRDEL
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分子量
46 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.
