Recombinant Human TAP protein

中文名： 胰蛋白酶原激活肽(TAP)重组蛋白
别名： TAP；ABCB2；PSF1；RING4；Antigen peptide transporter 1

货号: PA1000-8896

Price： ￥询价

20μg 50μg 100μg ＞100μg

数量：

大包装询价

产品详情

纯度	>90%SDS-PAGE.
种属	Human
靶点	TAP
Uniprot No	Q03518
内毒素	< 0.01EU/μg
表达宿主	E.coli
表达区间	1-808aa
氨基酸序列	MAELLASAGSACSWDFPRAPPSFPPPAASRGGLGGTRSFRPHRGAESPRP GRDRDGVRVPMASSRCPAPRGCRCLPGASLAWLGTVLLLLADWVLLRTAL PRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGSKSENAGAQ GWLAALKPLAAALGLALPGLALFRELISWGAPGSADSTRLLHWGSHPTAF VVSYAAALPAAALWHKLGSLWVPGGQGGSGNPVRRLLGCLGSETRRLSLF LVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAV LEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNIMSRVTE DTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLITLPLLFL LPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKF REKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPP SGLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPN GSGKSTVAALLQNLYQPTGGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQV FGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVDEAG SQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPE RYSRSVLLITQHLSLVEQADHILFLEGGAIREGGTHQQLMEKKGCYWAMV QAPADAPE
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3-4条关于TAP(Tandem Affinity Purification)重组蛋白技术的参考文献及摘要概括：

1. **"A generic protein purification method for protein complex characterization and proteome exploration"**

- **作者**: Rigaut, G., et al. (1999)

- **摘要**: 提出TAP技术，通过融合双标签(钙调蛋白结合肽和IgG结合结构域)实现重组蛋白及其相互作用复合体的高效纯化，适用于酵母和大肠杆菌系统。

2. **"Functional organization of the yeast proteome by systematic analysis of protein complexes"**

- **作者**: Gavin, A.C., et al. (2002)

- **摘要**: 结合TAP技术与质谱分析，系统鉴定了酵母中的蛋白质相互作用网络，揭示了多蛋白复合体的功能组织框架。

3. **"The tandem affinity purification (TAP) method: a general procedure of protein complex purification"**

- **作者**: Puig, O., et al. (2001)

- **摘要**: 详细优化TAP技术流程，提高了重组蛋白复合体纯化的特异性和效率，并验证其在真核细胞中的应用潜力。

4. **"TAP purification strategy in mammalian cells reveals novel protein interactions of the mTOR pathway"**

- **作者**: Drakas, R., et al. (2005)

- **摘要**: 将TAP技术应用于哺乳动物细胞，成功分离mTOR信号通路相关蛋白复合体，揭示了新的调控因子和相互作用网络。

这些文献涵盖了TAP技术的开发、优化及在不同生物体系中的应用，适合作为重组蛋白纯化和相互作用研究的参考。

背景信息

**Background of TAP-Tagged Recombinant Proteins**

Tandem Affinity Purification (TAP)-tagged recombinant proteins emerged in the late 1990s as a breakthrough tool for studying protein complexes under near-native conditions. Developed initially in yeast, the TAP system was designed to enable efficient purification of multi-protein assemblies with high specificity while minimizing disruption to cellular interactions. The core innovation lies in the dual-affinity tag fused to the target protein. A typical TAP tag combines two distinct affinity modules—originally Protein A (binding immunoglobulin G) and a calmodulin-binding peptide (CBP)—separated by a cleavage site for the tobacco etch virus (TEV) protease.

The purification process involves two sequential steps. First, the Protein A moiety binds to IgG-coated beads, allowing initial capture of the tagged protein and its interacting partners. After TEV protease cleavage releases the complex, the second purification via CBP-calmodulin interaction further eliminates nonspecific bindings. This two-step strategy significantly enhances purity compared to single-affinity methods.

TAP-tagged systems gained popularity due to their versatility and compatibility with diverse organisms, including mammalian cells. They enabled large-scale interactome studies, revealing dynamic protein networks in processes like transcription, signaling, and metabolism. Moreover, the gentle elution conditions preserved labile interactions and enzymatic activities, making TAP ideal for functional analyses.

Advances in mass spectrometry later synergized with TAP tagging, allowing sensitive identification of co-purified proteins. Despite competition from newer techniques like proximity-dependent biotinylation (e.g., BioID), TAP remains relevant for its balanced specificity and yield, particularly in characterizing stable complexes. Modern variants now incorporate alternative tags (e.g., Strep-tag, FLAG) or inducible expression systems to study context-dependent interactions, sustaining its role in proteomics and structural biology research.