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UBE2Q2/UBE2Q2蛋白Recombinant Hum

an Ubiquitin-conjugating enzyme E2 Q2 (UBE2Q2)重组蛋白Ubiquitin carrier protein Q2Ubiquitin-protein ligase Q2蛋白
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  • ¥1344 - 10872
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  • CN
  • CSB-EP845153HU
  • 2025年07月14日
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    • 详细信息
    • 文献和实验
    • 技术资料
    • 保存条件

      Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

    • 保质期

      Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

    • 英文名

      Recombinant Human Ubiquitin-conjugating enzyme E2 Q2 (UBE2Q2)

    • 库存

      200

    • 供应商

      武汉华美生物工程有限公司

    • 规格

      1mg/100μg/20μg

    规格:1mg产品价格:¥10872.0
    规格:100μg产品价格:¥2514.0
    规格:20μg产品价格:¥1344.0

    纯度:

    Greater than 90% as determined by SDS-PAGE.

    基因名:

    UBE2Q2

    Uniprot No.:

    Q8WVN8

    别名:

    Ubiquitin carrier protein Q2Ubiquitin-protein ligase Q2

    种属:

    Homo sapiens (Human)

    蛋白长度:

    Full Length

    来源:

    E.coli

    分子量:

    58.8 kDa

    表达区域:

    1-375aa

    氨基酸序列:

    MSVSGLKAELKFLASIFDKNHERFRIVSWKLDELHCQFLVPQQGSPHSLPPPLTLHCNITESYPSSSPIWFVDSEDPNLTSVLERLEDTKNNNLLRQQLKWLICELCSLYNLPKHLDVEMLDQPLPTGQNGTTEEVTSEEEEEEEEMAEDIEDLDHYEMKEEEPISGKKSEDEGIEKENLAILEKIRKTQRQDHLNGAVSGSVQASDRLMKELRDIYRSQSYKTGIYSVELINDSLYDWHVKLQKVDPDSPLHSDLQILKEKEGIEYILLNFSFKDNFPFDPPFVRVVLPVLSGGYVLGGGALCMELLTKQGWSSAYSIESVIMQINATLVKGKARVQFGANKNQYNLARAQQSYNSIVQIHEKNGWYTPPKEDG

    蛋白标签:

    N-terminal 6xHis-SUMO-tagged

    产品提供形式:

    Liquid or Lyophilized powder

    缓冲液:

    If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

    货期:

    13-23 business days

    注意事项:

    Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.

    功能:

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination.

    内毒素:

    Not test.

    SDS-PAGE:

    (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

    LC-MS Image Description/Western Blot:

    /

    Product types:

    Developed Protein

    Biological_Activity:

    /

    Research Areas:

    Epigenetics and Nuclear Signaling

    Reconstitution:

    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

    Reference:

    Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004)

    Function:

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination.

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    图标文献和实验
    该产品被引用文献
    Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004)
    相关实验
    • Studies of the Ubiquitin Proteasome System

      in Insect Cells Using a Baculovirus System Alternate Protocol 11: Preparation of Rabbit E1 Support Protocol 4: Generation of Empty Bacterial Lysates Generation of UbiquitinConjugating Enzymes (E2s) Basic Protocol 22: Expression of E2s in E. coli

    • A High‐Throughput Screening Method for Identification of Inhibitors of the Deubiquitinating Enzyme USP14

      Proteasomes that Lack Endogenous USP14 and are Devoid of UB‐AMC Hydrolysis Activity Support Protocol 2: Purification of Recombinant Human USP14 from E. coli Support Protocol 3: Synthesis and Purification of Ubiquitin

    • Rho1D4纯化体系:专为重组膜蛋白提取设计

      特异性结合的单克隆抗体1。与Rho1D4抗体结合的表位可以作为针对膜蛋白的超高特异性纯化标记。通过基因修饰可在欲研究的目标(膜)蛋白C端加上Rho1D4标记。一旦加载上该序列,即可用装载有Rho1D4抗体的亲和基质去捕获目标蛋白,随后添加Rho1D4肽,通过竞争性结合基质抗体的方式来洗脱目标蛋白。采用这种方法,相比改变pH值等其他洗脱方式,更加地温和。图1:假设有3个跨膜域的膜蛋白。Rho1D4标签加到膜蛋白C端,它的序列是T-E-T-S-Q-V-A-P-A2) Rho1D4的历史Rho1D4的表位

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    文献支持
    UBE2Q2/UBE2Q2蛋白Recombinant Human Ubiquitin-conjugating enzyme E2 Q2 (UBE2Q2)重组蛋白Ubiquitin carrier protein Q2Ubiquitin-protein ligase Q2蛋白
    ¥1344 - 10872