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Recombinant Human HSPA2 protein

  • 中文名: 70kDa热休克蛋白2(HSPA2)重组蛋白
  • 别    名: HSPA2;Heat shock-related 70 kDa protein 2
货号: PA1000-7615
Price: ¥询价
数量:
大包装询价

产品详情

纯度>90%SDS-PAGE.
种属Human
靶点HSPA2
Uniprot No P54652
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-639aa
氨基酸序列MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG ETKTFFPEEI SSMVLTKMKE IAEAYLGGKV HSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM VSHLAEEFKR KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA AKNALESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK ELERVCNPII SKLYQGGPGG GSGGGGSGAS GGPTIEEVD
预测分子量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HSPA2重组蛋白的3篇文献示例(内容为模拟概括,仅供参考):

1. **文献名称**:*Recombinant HSPA2 enhances sperm motility and DNA integrity in vitro*

**作者**:Smith A, et al.

**摘要**:研究通过大肠杆菌表达重组HSPA2蛋白,验证其在体外对精子功能的影响,发现其能显著改善精子活力和减少DNA损伤,提示HSPA2在男性不育治疗中的潜在应用。

2. **文献名称**:*HSPA2 overexpression promotes cancer cell survival via PI3K/Akt signaling pathway*

**作者**:Chen L, et al.

**摘要**:利用重组HSPA2蛋白进行细胞实验,发现其通过激活PI3K/Akt通路抑制肿瘤细胞凋亡,为靶向HSPA2的癌症治疗提供理论依据。

3. **文献名称**:*Purification and functional characterization of human HSPA2 recombinant protein*

**作者**:Wang Y, et al.

**摘要**:报道了一种高效的HSPA2重组蛋白纯化方法,并通过体外实验证实其分子伴侣活性,为后续机制研究奠定基础。

(注:以上文献为示例,实际引用需根据真实数据库检索结果调整。)

背景信息

**Background of HSPA2 Recombinant Protein**

HSPA2. a member of the heat shock protein 70 (HSP70) family, is a molecular chaperone critical for cellular stress responses, protein folding, and quality control. It shares structural and functional homology with other HSP70 proteins but exhibits unique expression patterns and roles in specific tissues. HSPA2 is highly expressed in the male germline, particularly during spermatogenesis, where it facilitates proper folding of proteins essential for sperm maturation and genomic stability. It also plays roles in cancer progression, neuroprotection, and cellular adaptation to environmental stressors like heat, oxidative damage, or chemotherapeutic agents.

Recombinant HSPA2 protein is produced using genetic engineering techniques, often in bacterial (e.g., *E. coli*) or eukaryotic expression systems (e.g., mammalian or insect cells). The process involves cloning the *HSPA2* gene into an expression vector, followed by transfection into host cells, induction of protein expression, and purification via affinity chromatography. The resulting recombinant protein retains the functional domains of native HSPA2. including the nucleotide-binding domain (NBD) and substrate-binding domain (SBD), enabling ATP-dependent substrate interactions.

Research on HSPA2 recombinant protein focuses on elucidating its molecular mechanisms in protein homeostasis, stress resilience, and disease. In cancer, HSPA2 overexpression correlates with tumor aggressiveness, metastasis, and chemoresistance, making it a potential therapeutic target. In reproductive biology, it is studied for its role in male infertility. Additionally, HSPA2's neuroprotective properties are explored in neurodegenerative disorders like Alzheimer’s disease.

The availability of recombinant HSPA2 facilitates *in vitro* assays, structural studies, and drug screening, advancing both basic science and translational applications. Its dual roles in cellular protection and pathology underscore its significance in biomedicine.

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