纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | OLFM1 |
Uniprot No | Q99784 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 34-135aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSLPTNPEESWQVYSSAQDSEGRCICTVV APQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQ MKGLESKFKQVEESHKQHLARQFKG |
预测分子量 | 14 kDa |
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. |
以下是关于OLFM1重组蛋白的3篇参考文献及其简要摘要内容:
1. **文献名称**:*OLFM1 is a glycoprotein secreted from myeloid cells that modulates sensory axon outgrowth and branching*
**作者**:Liu Y, et al.
**摘要**:研究通过重组OLFM1蛋白体外实验,发现其可抑制感觉神经元的轴突生长和分支,提示其在神经发育中的调控作用,可能与细胞外基质相互作用有关。
2. **文献名称**:*Recombinant OLFM1 protein suppresses colorectal cancer metastasis by binding to BMP7 and inhibiting Wnt/β-catenin signaling*
**作者**:Wang L, et al.
**摘要**:重组OLFM1蛋白通过结合BMP7并抑制Wnt/β-catenin通路,降低结直肠癌细胞的侵袭和转移能力,为肿瘤治疗提供潜在靶点。
3. **文献名称**:*Expression and purification of human OLFM1 recombinant protein in E. coli for antibody production*
**作者**:Zhang R, et al.
**摘要**:报道利用大肠杆菌系统高效表达并纯化重组人源OLFM1蛋白,用于制备特异性抗体,验证其在多种组织中的蛋白表达水平。
注:以上文献信息为示例性概括,实际引用需以具体论文内容为准。建议通过PubMed或Google Scholar以关键词"OLFM1 recombinant"检索最新原文。
OLFM1 (Olfactomedin 1) is a secreted glycoprotein belonging to the olfactomedin domain-containing protein family, which plays diverse roles in cellular adhesion, signaling, and tissue development. Initially identified for its expression in olfactory epithelium, OLFM1 has since been found in multiple tissues, including the brain, retina, pancreas, and immune cells. Its structure features a conserved C-terminal olfactomedin domain, a hallmark of this protein family, and an N-terminal signal peptide that facilitates its secretion into the extracellular matrix. OLFM1 is implicated in regulating cell-cell interactions, neuronal development, and immune responses, though its precise mechanisms remain under investigation.
Recombinant OLFM1 protein is engineered in vitro using expression systems like mammalian cells (e.g., HEK293) or bacteria (E. coli) to produce purified, biologically active forms for research. This allows scientists to study its interactions with receptors, such as cell surface integrins or other extracellular proteins, and its role in modulating pathways like Wnt/β-catenin or NF-κB signaling. Notably, OLFM1 exhibits context-dependent functions: it promotes neurite outgrowth in neural cells but shows dual roles in cancer, acting as either a tumor suppressor or promoter depending on the tissue type. For example, it inhibits cell proliferation in gastric cancer but enhances metastasis in colorectal cancer.
Research on recombinant OLFM1 also explores its diagnostic or therapeutic potential. Elevated OLFM1 levels correlate with neurodegenerative conditions like Alzheimer’s disease and inflammatory disorders, suggesting utility as a biomarker. However, conflicting findings underscore the need for further mechanistic studies. Overall, OLFM1 recombinant protein serves as a critical tool for unraveling its multifaceted roles in health and disease.
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