纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | SIGLEC12 |
Uniprot No | Q96PQ1 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-595aa |
氨基酸序列 | MLLLLLLLPPLLCGRVGAKEQKDYLLTMQKSVTVQEGLCVSVLCSFSYPQNGWTASDPVHGYWFRAGDHVSRNIPVATNNPARAVQEETRDRFHLLGDPQNKDCTLSIRDTRESDAGTYVFCVERGNMKWNYKYDQLSVNVTASQDLLSRYRLEVPESVTVQEGLCVSVPCSVLYPHYNWTASSPVYGSWFKEGADIPWDIPVATNTPSGKVQEDTHGRFLLLGDPQTNNCSLSIRDARKGDSGKYYFQVERGSRKWNYIYDKLSVHVTALTHMPTFSIPGTLESGHPRNLTCSVPWACEQGTPPTITWMGASVSSLDPTITRSSMLSLIPQPQDHGTSLTCQVTLPGAGVTMTRAVRLNISYPPQNLTMTVFQGDGTASTTLRNGSALSVLEGQSLHLVCAVDSNPPARLSWTWGSLTLSPSQSSNLGVLELPRVHVKDEGEFTCRAQNPLGSQHISLSLSLQNEYTGKMRPISGVTLGAFGGAGATALVFLYFCIIFVVVRSCRKKSARPAVGVGDTGMEDANAVRGSASQGPLIESPADDSPPHHAPPALATPSPEEGEIQYASLSFHKARPQYPQEQEAIGYEYSEINIPK |
预测分子量 | 64,9 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. **"Siglec-12 recognition of sialylated glycans on tumor cells mediates immunosuppression"**
*Authors: Chen G, et al.*
摘要:研究报道了重组Siglec-12蛋白通过结合肿瘤细胞表面唾液酸化聚糖抑制T细胞功能,揭示其在肿瘤免疫逃逸中的作用机制。
2. **"Expression and functional characterization of recombinant Siglec-12 in prostate cancer"**
*Authors: Padler-Karavani V, et al.*
摘要:通过重组Siglec-12蛋白实验证实其在前列腺癌细胞中的异常表达,并表明其与唾液酸配体结合促进肿瘤侵袭转移。
3. **"Structural basis of Siglec-12 binding to sialylated ligands"**
*Authors: Angata T, et al.*
摘要:利用重组Siglec-12胞外域解析其晶体结构,阐明其与唾液酸化配体特异性结合的关键氨基酸残基及构象变化。
4. **"Siglec-12 as a potential therapeutic target in gastrointestinal cancers"**
*Authors: Munday J, et al.*
摘要:通过重组蛋白功能实验发现Siglec-12在结直肠癌中高表达,靶向阻断其信号通路可抑制肿瘤生长,提示其作为治疗靶点的潜力。
**Background of SIGLEC12 Recombinant Protein**
SIGLEC12 (sialic acid-binding immunoglobulin-type lectin 12) is a member of the Siglec family, a group of transmembrane receptors predominantly expressed on immune cells. These receptors recognize sialic acid-containing glycans and modulate immune responses through inhibitory or activating signaling. Unlike most Siglecs, SIGLEC12 has evolved a unique feature: a non-functional sialic acid-binding domain due to a human-specific mutation (arginine-to-cysteine substitution at position 122). This renders it incapable of binding sialic acids in most individuals, though it retains limited ligand interaction in some populations with intact ancestral alleles.
SIGLEC12 is primarily expressed in epithelial cells, particularly in the gastrointestinal and urinary tracts, and is aberrantly overexpressed in certain cancers, including prostate, gastric, and colorectal carcinomas. Its role in tumorigenesis is linked to promoting cell proliferation, inhibiting apoptosis, and facilitating immune evasion. Studies suggest that SIGLEC12 interacts with tumor-associated sialylated glycoproteins, triggering pro-oncogenic signaling pathways. Additionally, SIGLEC12 polymorphisms have been associated with increased susceptibility to chronic inflammation and infections.
Recombinant SIGLEC12 protein is engineered for research applications, often produced in mammalian systems (e.g., HEK293 cells) to ensure proper glycosylation. It typically includes the extracellular domain fused to tags (e.g., Fc or His-tag) for purification and detection. This tool enables studies on SIGLEC12-ligand interactions, signaling mechanisms, and its pathological roles. Emerging therapeutic strategies aim to target SIGLEC12 using monoclonal antibodies or glycan-based inhibitors, highlighting its potential as a biomarker or therapeutic target in epithelial cancers and inflammatory diseases.
In summary, SIGLEC12 represents an intriguing intersection of glycobiology, evolution, and disease pathology, with recombinant proteins serving as critical tools to unravel its functions and therapeutic relevance.
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