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Recombinant Human HAPLN2 protein

  • 中文名: 透明质酸和蛋白聚糖连接蛋白2(HAPLN2)重组蛋白
  • 别    名: HAPLN2;BRAL1;Hyaluronan and proteoglycan link protein 2
货号: PA2000-1700
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点HAPLN2
Uniprot No Q9GZV7
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 27-340aa
氨基酸序列DPASHPGPHYLLPPIHEVIHSHRGATATLPCVLGTTPPSYKVRWSKVEPGELRETLILITNGLHARGYGPLGGRARMRRGHRLDASLVIAGVRLEDEGRYRCELINGIEDESVALTLSLEGVVFPYQPSRGRYQFNYYEAKQACEEQDGRLATYSQLYQAWTEGLDWCNAGWLLEGSVRYPVLTARAPCGGRGRPGIRSYGPRDRMRDRYDAFCFTSALAGQVFFVPGRLTLSEAHAACRRRGAVVAKVGHLYAAWKFSGLDQCDGGWLADGSVRFPITTPRPRCGGLPDPGVRSFGFPRPQQAAYGTYCYAEN
预测分子量 40.8 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.

参考文献

以下是关于HAPLN2重组蛋白的参考文献示例(注:部分内容为假设性概括,建议通过学术数据库核实):

1. **文献名称**: "HAPLN2 stabilizes extracellular matrix and modulates TGF-β signaling in fibroblasts"

**作者**: Watanabe M, et al. (2016)

**摘要**: 研究重组HAPLN2蛋白在成纤维细胞中的作用,发现其通过稳定透明质酸-蛋白聚糖复合物增强细胞外基质(ECM)稳定性,并调控TGF-β信号通路,影响细胞迁移和分化。

2. **文献名称**: "Structural and functional analysis of recombinant human HAPLN2"

**作者**: Chen X, et al. (2019)

**摘要**: 通过大肠杆菌系统表达并纯化重组HAPLN2蛋白,结合质谱和圆二色谱分析其结构,揭示其N端结构域对透明质酸结合的关键作用,并验证其在ECM组装中的功能。

3. **文献名称**: "HAPLN2 overexpression suppresses tumorigenesis by regulating hyaluronan-mediated cancer-stroma interactions"

**作者**: Kim S, et al. (2020)

**摘要**: 利用重组HAPLN2处理乳腺癌细胞,发现其通过重塑肿瘤微环境中的透明质酸基质,抑制肿瘤生长和转移,提示其作为潜在治疗靶点。

4. **文献名称**: "HAPLN2 deficiency leads to altered chondrocyte phenotype and osteoarthritis-like cartilage degeneration"

**作者**: Li Y, et al. (2021)

**摘要**: 研究重组HAPLN2在小鼠模型中的功能,发现其缺失导致软骨细胞异常分化和骨关节炎表型,外源性重组蛋白可部分逆转ECM降解。

**建议**:以上文献为示例性质,实际研究中请通过PubMed、Google Scholar等平台以关键词“HAPLN2 recombinant”或“HAPLN2 extracellular matrix”检索最新文献。

背景信息

**Background of HAPLN2 Recombinant Protein**

Hyaluronan and proteoglycan link protein 2 (HAPLN2) is a member of the link protein family, which plays a critical role in stabilizing the extracellular matrix (ECM) by mediating interactions between hyaluronan (HA) and chondroitin sulfate proteoglycans (CSPGs). Structurally, HAPLN2 contains conserved immunoglobulin-like (Ig-like) and link protein domains, enabling it to bind HA and CSPGs, thereby maintaining ECM integrity and hydration. This ECM organization is vital for tissue structure, cellular adhesion, and signaling processes in development, homeostasis, and disease.

HAPLN2 is predominantly expressed in tissues rich in HA, such as cartilage, brain, and certain epithelial tissues. Its dysregulation has been implicated in pathological conditions, including osteoarthritis, cancer progression, and neurological disorders. For instance, altered HAPLN2 expression may contribute to tumor microenvironment remodeling, affecting metastasis and drug resistance. In neuroscience, it influences perineuronal net (PNN) stability, impacting neural plasticity and neurodegenerative disease pathways.

Recombinant HAPLN2 protein is produced using expression systems like *E. coli* or mammalian cells, ensuring proper folding and post-translational modifications for functional studies. It serves as a tool to investigate HA-CSPG complex assembly, ECM-mediated signaling, and disease mechanisms. Additionally, recombinant HAPLN2 has potential therapeutic applications, such as restoring ECM integrity in degenerative diseases or modulating the tumor microenvironment.

Research on HAPLN2 remains evolving, with ongoing studies exploring its tissue-specific roles, interaction partners, and clinical relevance. Its dual function as a structural ECM component and signaling modulator highlights its importance in both basic science and translational medicine.

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