| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FCRL4 |
| Uniprot No | Q96PJ5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-387aa |
| 氨基酸序列 | AHKPVISVHPPWTTFFKGERVTLTCNGFQFYATEKTTWYHRHYWGEKLTLTPGNTLEVRESGLYRCQARGSPRSNPVRLLFSSDSLILQAPYSVFEGDTLVLRCHRRRKEKLTAVKYTWNGNILSISNKSWDLLIPQASSNNNGNYRCIGYGDENDVFRSNFKIIKIQELFPHPELKATDSQPTEGNSVNLSCETQLPPERSDTPLHFNFFRDGEVILSDWSTYPELQLPTVWRENSGSYWCGAETVRGNIHKHSPSLQIHVQRIPVSGVLLETQPSGGQAVEGEMLVLVCSVAEGTGDTTFSWHREDMQESLGRKTQRSLRAELELPAIRQSHAGGYYCTADNSYGPVQSMVLNVTVRETPGNRDGL |
| 预测分子量 | 43.6 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. |
1. **"FCRL4: An Emerging Biomarker in B-Cell Malignancies"**
- Authors: Li, F.J., et al.
- 摘要：研究报道了重组FCRL4蛋白在B细胞淋巴瘤中的表达及功能，证实其通过调控BCR信号通路促进恶性B细胞存活，为潜在治疗靶点。
2. **"Structural Insights into FCRL4-Mediated Immune Regulation"**
- Authors: Davis, R.S., & Wilson, T.J.
- 摘要：利用重组FCRL4蛋白进行晶体结构解析，揭示了其胞外域独特的Ig样结构域构象，阐明其与免疫复合物结合的分子机制。
3. **"Recombinant FCRL4 Protein Modulates B-Cell Activation in Autoimmunity"**
- Authors: Leu, C.M., & Sutton, H.J.
- 摘要：通过原核系统表达重组FCRL4.证明其抑制B细胞过度活化，在自身免疫模型小鼠中降低炎症因子水平，提示其免疫调节潜力。
4. **"FCRL4 Interaction with MHC Class II in Chronic Viral Infection"**
- Authors: Ehrhardt, G.R., et al.
- 摘要：重组FCRL4蛋白被用于体外结合实验，发现其特异性结合MHC II类分子，可能参与慢性病毒感染中B细胞的功能耗竭。
注：以上文献为虚拟示例，实际引用时需核对真实出版物信息。
Fc receptor-like 4 (FCRL4) is a transmembrane protein belonging to the Fc receptor-like (FCRL) family, which shares structural homology with classical Fc receptors but lacks direct Fc-binding capacity. Primarily expressed in subsets of B lymphocytes, particularly memory B cells and certain B-cell malignancies, FCRL4 has emerged as a key regulator of immune responses. Its expression is tightly regulated during B-cell differentiation, with elevated levels observed in tissue-resident B cells at mucosal sites, suggesting a role in mucosal immunity or pathogen interaction.
Structurally, FCRL4 contains multiple extracellular immunoglobulin-like domains and cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs), enabling it to modulate B-cell receptor (BCR) signaling. Studies indicate that FCRL4 acts as a checkpoint molecule, dampening B-cell activation and proliferation through ITIM-mediated recruitment of phosphatases like SHP-1/SHP-2. This suppressive function positions FCRL4 as a potential therapeutic target in autoimmune disorders or B-cell lymphomas characterized by dysregulated signaling.
Recombinant FCRL4 proteins, typically produced in mammalian expression systems to ensure proper glycosylation and folding, are crucial tools for studying receptor-ligand interactions, signaling mechanisms, and drug development. These proteins often include epitope tags (e.g., Fc or His tags) for purification and detection. Recent research highlights FCRL4's interaction with unidentified ligands in microbial pathogens, suggesting a role in host-pathogen crosstalk. Additionally, its overexpression in chronic lymphocytic leukemia and HIV-associated B-cell dysfunction underscores its clinical relevance. Recombinant FCRL4 enables structural studies (e.g., crystallography) and high-throughput screening for inhibitors/agonists, bridging basic immunology and translational applications.
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