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Recombinant Human Proteasome 2

6S Subunit, Non-ATPase 5
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  • ¥1080 - 45885
  • Prospecbio
  • 以色列
  • enz-914
  • 2026年01月06日
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    • 详细信息
    • 文献和实验
    • 技术资料
    • 保存条件

      for future use below -18°C

    • 保质期

      See instructions

    • 英文名

      PSMD5

    • 库存

      常规产品有备货

    • 供应商

      上海经科化学科技有限公司

    • CAS号

    • 规格

      5ug/20ug/1mg

    规格:5ug产品价格:¥1080.0
    规格:20ug产品价格:¥2415.0
    规格:1mg产品价格:¥45885.0

    产品细节图片1

    CATALOGUE NUMBER

    ENZ-914

    SYNONYMS

    PSMD5, Proteasome (Prosome, Macropain) 26S Subunit, Non-ATPase, 526S Protease Subunit S5 Basic,26S Proteasome Subunit S5B,S5B,26S Proteasome Non-ATPase Regulatory Subunit 5,KIAA0072.

    INTRODUCTION

    Proteasome 26S Subunit, Non-ATPase 5, also known as PSMD5 is a member of the proteasome subunit S5B/HSM3 family. The 26S proteasome is an enzymatic complex which degrades ubiquitinated proteins in eukaryotic cells. Furthermore, PSMD5 acts as a chaperones which is involved in the assembly of the 26s proteasome, particularly of the base subcomplex of the PA700/19S regulatory complex. PSMD5 is full of dileucine repeats, which have been involved in trafficking of various transmembrane proteins.

    DESCRIPTION

    PSMD5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 529 amino acids (1-504 a.a) and having a molecular mass of 58.9kDa.
    PSMD5 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    SOURCE

    E.coli.

    PHYSICAL APPEARANCE

    Sterile Filtered colorless solution.

    FORMULATION

    PSMD5 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    STABILITY

    Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.
    For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
    Avoid multiple freeze-thaw cycles.

    PURITY

    Greater than 90.0% as determined by SDS-PAGE.

    AMINO ACID SEQUENCE

    MG./S-SHHHHHH SSGLVPRGSH MGSEFMAAQA LALLREVARL EAPLEELRAL HSVLQAVPLN ELRQQAAELR LGPLFSLLNE NHREKTTLCV SILERLLQAM EPVHVARNLR VDLQRGLIHP DDSVKILTLS QIGRIVENSD AVTEILNNAE LLKQIVYCIG GENLSVAKAA IKSLSRISLT QAGLEALFES NLLDDLKSVM KTNDIVRYRV YELIIEISSV SPESLNYCTT SGLVTQLLRE LTGEDVLVRA TCIEMVTSLA YTHHGRQYLA QEGVIDQISN IIVGADSDPF SSFYLPGFVK FFGNLAVMDS PQQICERYPI FVEKVFEMIE SQDPTMIGVA VDTVGILGSN VEGKQVLQKT GTRFERLLMR IGHQSKNAPV ELKIRCLDAI SSLLYLPPEQ QTDDLLRMTE SWFSSLSRDP LELFRGISSQ PFPELHCAAL KVFTAIANQP WAQKLMFNSP GFVEYVVDRS VEHDKASKDA KYELVKALAN SKTIAEIFGN PNYLRLRTYL SEGPYYVKPV STTAVEGAE.

    SAFETY DATA SHEET

    SDS

    USAGE

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
     

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    图标文献和实验
    该产品被引用文献

    PSMD5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 529 amino acids (1-504 a.a) and having a molecular mass of 58.9kDa.

    PSMD5 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
    相关实验
    • Studies of the Ubiquitin Proteasome System

      of Unstable E3s in Bacterial Lysates Basic Protocol 25: Expression of E3s in Eukaryotic in Vitro Translation Systems Basic Protocol 26: Expression of Multi‐Subunit E3s Using a Baculovirus Expression System Support Protocol 5: Batch Purification of Multimeric E

    • Selection of Non-aggregating VH Binders from Synthetic VH Phage-Display Libraries

      approaches for developing non-aggregating human VH s with binding specificities have relied on a combination of recombinant DNA technology and phage-display technology. VH gene libraries are constructed synthetically by randomizing the CDRs of a single VH

    • Recombinant Adeno-Associated Viral Vector Production and Purification

      . In general, AAV vectors lead to robust, long-term in vivo transduction in rodents, dogs, and non-human primates. To meet specific research needs, investigators have developed numerous AAV variants by engineering viral capsid and/or genome. Here we outline

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