| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSP90B1 |
| Uniprot No | P14625 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-799aa |
| 氨基酸序列 | VDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKKPKTKKVEKTVWDWELMNDIKPIWQRPSKEVEEDEYKAFYKSFSKESDDPMAYIHFTAEGEVTFKSILFVPTSAPRGLFDEYGSKKSDYIKLYVRRVFITDDFHDMMPKYLNFVKGVVDSDDLPLNVSRETLQQHKLLKVIRKKLVRKTLDMIKKIADDKYNDTFWKEFGTNIKLGVIEDHSNRTRLAKLLRFQSSHHPTDITSLDQYVERMKEKQDKIYFMAGSSRKEAESSPFVERLLKKGYEVIYLTEPVDEYCIQALPEFDGKRFQNVAKEGVKFDESEKTKESREAVEKEFEPLLNWMKDKALKDKIEKAVVSQRLTESPCALVASQYGWSGNMERIMKAQAYQTGKDISTNYYASQKKTFEINPRHPLIRDMLRRIKEDEDDKTVLDLAVVLFETATLRSGYLLPDTKAYGDRIERMLRLSLNIDPDAKVEEEPEEEPEETAEDTTEDTEQDEDEEMDVGTDEEEETAKESTAE |
| 预测分子量 | 93.1kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于HSP90B1(GRP94)重组蛋白的关键文献概览：
1. **文献名称**：*Molecular Cloning and Characterization of GRP94. a Glucose-regulated Endoplasmic Reticulum Protein*
**作者**：Kozutsumi Y. et al.
**摘要**：首次报道了HSP90B1(GRP94)的基因克隆及重组表达，阐明其作为内质网分子伴侣在葡萄糖饥饿应激下的调控机制，并验证其与免疫球蛋白重链的折叠关联。
2. **文献名称**：*GRP94: A Target for Cancer Therapy*
**作者**：Niessen M. et al.
**摘要**：研究重组HSP90B1蛋白在肿瘤微环境中的作用，发现其通过调控EGFR/AKT信号通路促进癌细胞存活，提出靶向GRP94抑制肿瘤生长的潜在治疗策略。
3. **文献名称**：*Structural Basis for the Interaction of GRP94 with Client Proteins*
**作者**：Marzec M. et al.
**摘要**：利用重组HSP90B1蛋白进行X射线晶体学分析，揭示其ATP结合域构象变化如何辅助客户蛋白(如Toll样受体)的正确折叠及功能调控。
4. **文献名称**：*Recombinant GRP94 as a Biomarker for Endoplasmic Reticulum Stress in Neurodegenerative Diseases*
**作者**：Wang Y. et al.
**摘要**：构建重组HSP90B1蛋白检测体系，证实其在阿尔茨海默病模型中与内质网应激标志物BiP共表达升高，提示其作为神经退行性疾病诊断标志物的潜力。
(注：以上文献为虚拟示例，实际引用需核对真实出版物信息。)
HSP90B1. also known as GRP94 or gp96. is a member of the heat shock protein 90 (HSP90) family. Unlike its cytosolic paralog HSP90AA1. HSP90B1 is primarily localized in the endoplasmic reticulum (ER), where it functions as a molecular chaperone. It plays a critical role in the folding, assembly, and quality control of secreted and membrane-bound proteins, including Toll-like receptors (TLRs), integrins, and immunoglobulins. Structurally, it shares the conserved N-terminal ATP-binding domain and C-terminal dimerization motif characteristic of HSP90 proteins, but its ER retention sequence (KDEL) ensures its localization within the ER lumen.
HSP90B1 operates in conjunction with other ER chaperones like BiP and calnexin, forming transient complexes to assist client protein maturation. Its ATP-dependent conformational changes enable substrate binding and release. Dysregulation of HSP90B1 is implicated in various pathologies, including cancer, inflammatory diseases, and autoimmune disorders. In tumors, its overexpression supports oncoprotein stability and promotes cell survival under hypoxic or nutrient-deprived conditions, making it a potential therapeutic target. Additionally, it acts as a key player in immune regulation by facilitating antigen presentation and activating innate immune responses through interactions with TLRs.
Recombinant HSP90B1 proteins are typically produced in mammalian or insect cell systems to ensure proper post-translational modifications (e.g., glycosylation) and functional folding. These recombinant forms are widely used in structural studies to elucidate chaperone-client interaction mechanisms, screen for inhibitors, and investigate ER stress pathways. In immunotherapy, recombinant HSP90B1 has been explored as an adjuvant to enhance antigen-specific immune responses due to its ability to bind and present antigenic peptides to dendritic cells.
Overall, HSP90B1’s dual roles in proteostasis and immunity underscore its significance in both basic research and therapeutic development.
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