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endoplasmic

" in MedChemExpress (MCE) Product Catalog:

127

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1

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11

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3

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32

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21

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12

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8

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Cat. No. Compare Product Name Species Source
  • HY-P72239
    HSPA5/GRP-78 Protein, Human (His)

    endoplasmic reticulum chaperone BiP; GRP-78; BiP; GRP78

    		 Human E. coli
    HSPA5/GRP-78 is an endoplasmic reticulum chaperone that coordinates protein folding and quality control. It cooperates with DNAJC10/ERdj5 to facilitate correct protein folding and participates in the degradation of misfolded proteins, potentially releasing DNAJC10/ERdj5. HSPA5/GRP-78 Protein, Human (His) is the recombinant human-derived HSPA5/GRP-78 protein, expressed by E. coli , with N-6*His labeled tag. The total length of HSPA5/GRP-78 Protein, Human (His) is 269 a.a., with molecular weight of ~33.6 kDa.
  • HY-P75756
    ERAP2 Protein, Human (HEK293, His)

    endoplasmic reticulum aminopeptidase 2; L-RAP; ERAP2; LRAP

    		 Human HEK293
    ERAP2 protein, a key aminopeptidase, plays a pivotal role in peptide trimming, crucial for generating peptides binding to HLA class I molecules. By selectively hydrolyzing basic residues like Arginine (Arg) and Lysine (Lys), ERAP2 precisely customizes longer precursor peptides, ensuring optimal length for effective presentation on MHC class I molecules. ERAP2 Protein, Human (HEK293, His) is the recombinant human-derived ERAP2 protein, expressed by HEK293, with N-His, N-10*His labeled tag. The total length of ERAP2 Protein, Human (HEK293, His) is 905 a.a., with molecular weight of 115-125 kDa.
  • HY-P71686
    ERP29 Protein, Human (GST)

    ERP29; C12orf8; ERP28endoplasmic reticulum resident protein 29; ERp29; endoplasmic reticulum resident protein 28; ERp28; endoplasmic reticulum resident protein 31; ERp31

    		 Human E. coli
    Contrary to expectations, the ERP29 protein does not exhibit disulfide isomerase activity. Its function is critical in the processing of secreted proteins within the endoplasmic reticulum (ER) and may contribute to the folding of proteins in this cellular compartment. ERP29 Protein, Human (GST) is the recombinant human-derived ERP29 protein, expressed by E. coli , with N-GST labeled tag. The total length of ERP29 Protein, Human (GST) is 212 a.a., with molecular weight of ~51.0 kDa.
  • HY-P72112
    Calreticulin/CALR Protein, Mouse (GST)

    CalrCalreticulin; CRP55; Calregulin; endoplasmic reticulum resident protein 60; ERp60; HACBP

    		 Mouse E. coli
    The calreticulin/CALR protein acts as a calcium-binding partner and promotes endoplasmic reticulum folding, assembly, and quality control. It interacts with monoglucosylated glycoproteins and mediates nuclear export of the NR3C1 DNA-binding domain. Calreticulin/CALR Protein, Mouse (GST) is the recombinant mouse-derived Calreticulin/CALR protein, expressed by E. coli , with N-GST labeled tag. The total length of Calreticulin/CALR Protein, Mouse (GST) is 399 a.a., with molecular weight of ~73.3 kDa.
  • HY-P71722
    Calreticulin/CALR Protein, Pig (P.pastoris, His)

    CALRCalreticulin; CRP55; Calregulin; endoplasmic reticulum resident protein 60; ERp60; HACBP

    		 Pig P. pastoris
    Calreticulin (CALR) is an essential calcium-binding chaperone involved in ER functions. It interacts with glycoproteins, facilitates NR3C1 nuclear export, regulates maternal gene expression, and aids in oocyte maturation. CALR is released during oocyte activation and prevents polyspermy. It forms an EIF2 complex with CELF1/CUGBP1, CALR3, EIF2S1, EIF2S2, HSP90B1, and HSPA5 and interacts with PDIA3/ERp57, SPACA9, TRIM21, PPIB, PDIA5, and CLCC1. Calreticulin/CALR Protein, Pig (P.pastoris, His) is the recombinant pig-derived Calreticulin/CALR protein, expressed by P. pastoris , with N-His labeled tag. The total length of Calreticulin/CALR Protein, Pig (P.pastoris, His) is 400 a.a., with molecular weight of ~48.6 kDa.
  • HY-P71113
    PDIA4 Protein, Human (HEK293, His)

    Protein Disulfide-Isomerase A4; endoplasmic Reticulum Resident Protein 70; ER Protein 70; ERp70; endoplasmic Reticulum Resident Protein 72; ER Protein 72; ERp-72; ERp72; PDIA4; ERP70; ERP72

    		 Human HEK293
    The PDIA4 protein plays a key role in the chaperone complex, cooperating with various proteins. This dynamic assembly, including DNAJB11, HSP90B1 and others, orchestrates complex cellular processes. PDIA4 Protein, Human (HEK293, His) is the recombinant human-derived PDIA4 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of PDIA4 Protein, Human (HEK293, His) is 625 a.a., with molecular weight of ~75.0 kDa.
  • HY-P71609
    TXNDC5 Protein, Human (GST)

    EndoPDI; endoplasmic reticulum protein ERp46; endoplasmic reticulum resident protein 46; Endothelial protein disulphide isomerase; ER protein 46; ERp46; Hcc 2; MGC3178; PDIA15; TLP46; TXND5_HUMAN; TXNDC 5; Txndc5

    		 Human E. coli
    TXNDC5 Protein, an endoplasmic reticulum lumen-based disulfide isomerase, crucially aids in forming disulfide bonds for protein stability and function. Its ability to reduce disulfide bonds in insulin highlights its role in intricate protein folding processes. TXNDC5's functional attributes make it a key player in preserving the structural integrity of endoplasmic reticulum proteins, contributing to cellular homeostasis. TXNDC5 Protein, Human (GST) is the recombinant human-derived TXNDC5 protein, expressed by E. coli , with N-GST labeled tag. The total length of TXNDC5 Protein, Human (GST) is 324 a.a., with molecular weight of ~63.2 kDa.
  • HY-P71721
    Calreticulin/CALR Protein, Mouse (P.pastoris, His)

    Calr; Calreticulin; CRP55; Calregulin; endoplasmic reticulum resident protein 60; ERp60; HACBP

    		 Mouse P. pastoris
    The calreticulin/CALR protein acts as a calcium-binding partner and promotes endoplasmic reticulum folding, assembly, and quality control. It interacts with monoglucosylated glycoproteins and mediates nuclear export of the NR3C1 DNA-binding domain. Calreticulin/CALR Protein, Mouse (P.pastoris, His) is the recombinant mouse-derived Calreticulin/CALR protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of Calreticulin/CALR Protein, Mouse (P.pastoris, His) is 399 a.a., with molecular weight of ~48.3 kDa.
  • HY-P71721Y
    Calreticulin/CALR Protein, Mouse (P.pastoris, His, solution)

    Calr; Calreticulin; CRP55; Calregulin; endoplasmic reticulum resident protein 60; ERp60; HACBP

    		 Mouse P. pastoris
    The calreticulin/CALR protein acts as a calcium-binding partner and promotes endoplasmic reticulum folding, assembly, and quality control. It interacts with monoglucosylated glycoproteins and mediates nuclear export of the NR3C1 DNA-binding domain. Calreticulin/CALR Protein, Mouse (P.pastoris, His, solution) is the recombinant mouse-derived Calreticulin/CALR protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of Calreticulin/CALR Protein, Mouse (P.pastoris, His, solution) is 399 a.a., with molecular weight of ~48.3 kDa.
  • HY-P71046
    TXNDC12 Protein, Human (HEK293, His)

    Thioredoxin Domain-Containing Protein 12; endoplasmic Reticulum Resident Protein 18; ER Protein 18; ERp18; endoplasmic Reticulum Resident Protein 19; ER Protein 19; ERp19; Thioredoxin-Like Protein p19; hTLP19; TXNDC12; TLP19

    		 Human HEK293
    The TXNDC12 protein is an important endoplasmic reticulum-localized protein disulfide bond reductase that plays a key role in promoting disulfide bond formation in client proteins. As an essential component of cellular machinery, TXNDC12 contributes to complex protein folding processes, highlighting its importance in maintaining correct protein structure and function. TXNDC12 Protein, Human (HEK293, His) is the recombinant human-derived TXNDC12 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of TXNDC12 Protein, Human (HEK293, His) is 142 a.a., with molecular weight of ~18.0 kDa.
  • HY-P70891
    ERP27 Protein, Human (HEK293, His)

    endoplasmic Reticulum Resident Protein 27; ER Protein 27; ERp27; ERP27; C12orf46

    		 Human HEK293
    The ERP27 protein has a unique role in that it can specifically bind unfolded proteins and recruit the protein disulfide isomerase PDIA3 to the substrate through the hydrophobic pocket in its C-terminal domain. This interaction implies that ERP27 is involved in the unfolding stress response and resolves challenges in cellular proteostasis. ERP27 Protein, Human (HEK293, His) is the recombinant human-derived ERP27 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of ERP27 Protein, Human (HEK293, His) is 248 a.a., with molecular weight of 32-38 kDa.
  • HY-P702453
    STING1 Protein, Mouse (Cell-Free, His)

    Stimulator of interferon genes protein; endoplasmic reticulum interferon stimulator; ERIS; Mediator of IRF3 activation; MMITA; Transmembrane protein 173

    		 Mouse E. coli Cell-free
    STING1 is a promoter of innate immune signaling, a key sensor of bacterial and viral cytoplasmic DNA, and promotes the production of type I interferons (IFN-α and IFN-β). This innate immune response is triggered in response to non-CpG double-stranded DNA delivered to the cytoplasm from various pathogens. STING1 Protein, Mouse (Cell-Free, His) is the recombinant mouse-derived STING1 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of STING1 Protein, Mouse (Cell-Free, His) is 378 a.a., with molecular weight of 48.9 kDa.
  • HY-P70893
    ERO1L Protein, Human (HEK293, His)

    ERO1-Like Protein Alpha; ERO1-L; ERO1-L-Alpha; endoplasmic Oxidoreductin-1-Like Protein; Oxidoreductin-1-L-Alpha; ERO1L

    		 Human HEK293
    ERO1L protein is an oxidoreductase that can effectively reoxidize P4HB/PDI in the endoplasmic reticulum and promote the formation of disulfide bonds. It transfers electrons to molecular oxygen, producing reactive oxygen species (ROS). ERO1L Protein, Human (HEK293, His) is the recombinant human-derived ERO1L protein, expressed by HEK293 , with C-6*His labeled tag. The total length of ERO1L Protein, Human (HEK293, His) is 445 a.a., with molecular weight of ~71.0 kDa.
  • HY-P71742
    HSPA5/GRP-78 Protein, Mouse (P.pastoris, His)

    Hspa5; Grp78; endoplasmic reticulum chaperone BiP; EC 3.6.4.10; 78kDa glucose-regulated protein; GRP-78; HSP70 family protein 5

    		 Mouse P. pastoris
    The HSPA5/GRP-78 protein is an endoplasmic reticulum chaperone involved in protein folding and quality control. It interacts with DNAJC10/ERdj5 to fold and degrade misfolded proteins. HSPA5/GRP-78 Protein, Mouse (P.pastoris, His) is the recombinant mouse-derived HSPA5/GRP-78 protein, expressed by P. pastoris , with N-6*His, N-His labeled tag. The total length of HSPA5/GRP-78 Protein, Mouse (P.pastoris, His) is 636 a.a., with molecular weight of ~72.5 kDa.
  • HY-P71742Y
    HSPA5/GRP-78 Protein, Mouse (P.pastoris, His, solution)

    Hspa5; Grp78; endoplasmic reticulum chaperone BiP; EC 3.6.4.10; 78kDa glucose-regulated protein; GRP-78; HSP70 family protein 5

    		 Mouse P. pastoris
    HSPA5/GRP-78 Protein serves as a crucial endoplasmic reticulum chaperone, playing a pivotal role in protein folding and quality control within the endoplasmic reticulum lumen. It engages in correct protein folding and participates in the degradation of misfolded proteins, collaborating with DNAJC10/ERdj5 to facilitate the release of DNAJC10/ERdj5 from its substrate. Furthermore, HSPA5/GRP-78 acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, it is recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, disrupting the dimerization of ERN1/IRE1 and consequently inactivating it. The accumulation of misfolded proteins triggers the release of HSPA5/BiP from ERN1/IRE1, allowing for homodimerization and the subsequent activation of ERN1/IRE1. Additionally, HSPA5/GRP-78 plays an auxiliary role in the post-translational transport of small presecretory proteins across the endoplasmic reticulum and may function as an allosteric modulator for the SEC61 channel-forming translocon complex. It is suggested to cooperate with SEC62 to enable the productive insertion of these precursors into the SEC61 channel. The protein appears to specifically regulate the translocation of precursors with inhibitory residues in their mature region, which weaken channel gating. Beyond its role in protein folding, HSPA5/GRP-78 may also contribute to apoptosis and cell proliferation. HSPA5/GRP-78 Protein, Mouse (P.pastoris, His, solution) is the recombinant mouse-derived HSPA5/GRP-78 protein, expressed by P. pastoris , with N-His labeled tag. The total length of HSPA5/GRP-78 Protein, Mouse (P.pastoris, His, solution) is 636 a.a., with molecular weight of ~72.5 kDa.
  • HY-P702272
    ERLIN1 Protein, Human (Cell-Free, His)

    Erlin-1; endoplasmic reticulum lipid raft-associated protein 1; Protein KE04; Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1; SPFH domain-containing protein 1

    		 Human E. coli Cell-free
    The ERLIN1 protein is an important component of the ERLIN1/ERLIN2 complex and plays a key role in mediating endoplasmic reticulum-associated degradation (ERAD) of the inositol 1,4,5-trisphosphate receptor (IP3R). In addition to participating in ERAD, ERLIN1 also regulates cellular cholesterol homeostasis by regulating the SREBP signaling pathway. ERLIN1 Protein, Human (Cell-Free, His) is the recombinant human-derived ERLIN1 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of ERLIN1 Protein, Human (Cell-Free, His) is 348 a.a., with molecular weight of 42.0 kDa.
  • HY-P71193
    PDIA6 Protein, Human (HEK293, His)

    Protein Disulfide-Isomerase A6; endoplasmic Reticulum Protein 5; ER Protein 5; ERp5; Protein Disulfide Isomerase P5; Thioredoxin Domain-Containing Protein 7; PDIA6; ERP5; P5; TXNDC7

    		 Human HEK293
    PDIA6 protein has molecular chaperone activity, which can inhibit the aggregation of misfolded proteins and contribute to quality control. It negatively regulates the unfolded protein response (UPR) by binding to ERN1 and inhibiting its signaling. PDIA6 Protein, Human (HEK293, His) is the recombinant human-derived PDIA6 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of PDIA6 Protein, Human (HEK293, His) is 421 a.a., with molecular weight of ~52.0 kDa.
  • HY-P70957
    MAN1B1 Protein, Human (HEK293, His)

    endoplasmic Reticulum Mannosyl-Oligosaccharide 1; 2-Alpha-Mannosidase; ER Alpha-1; 2-Mannosidase; ER Mannosidase 1; ERMan1; Man9GlcNAc2-Specific-Processing Alpha-Mannosidase; Mannosidase Alpha Class 1B Member 1; MAN1B1

    		 Human HEK293
    MAN1B1, integral to glycoprotein quality control, trims a single alpha-1,2-linked mannose from Man(9)GlcNAc(2), producing Man(8)GlcNAc(2). In the ERQC, elevated enzyme concentrations allow further trimming to Man(5-6)GlcNAc(2). This enzymatic function is crucial for glycoprotein processing and quality control in the endoplasmic reticulum, ensuring proper folding and maturation. MAN1B1 Protein, Human (HEK293, His) is the recombinant human-derived MAN1B1 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of MAN1B1 Protein, Human (HEK293, His) is 594 a.a., with molecular weight of 58-80 kDa.
  • HY-P72111
    Calreticulin/CALR Protein, Human (His)

    Autoantigen RO; CALR; CALR protein; CALR_HUMAN; Calregulin; Calreticulin; cC1qR; CRP55; CRT; CRTC; endoplasmic reticulum resident protein 60; Epididymis secretory sperm binding protein Li 99n; ERp60; FLJ26680; grp60; HACBP; HEL S 99n; RO; Sicca syndrome antigen A autoantigen Ro; calreticulin; ; Sicca syndrome antigen A; SSA

    		 Human E. coli
    The calreticulin/CALR protein is a calcium-binding molecular chaperone that promotes ER folding and quality control. It interacts with monoglucosylated glycoproteins and promotes nuclear export of NR3C1. Calreticulin/CALR Protein, Human (His) is the recombinant human-derived Calreticulin/CALR protein, expressed by E. coli , with N-6*His labeled tag. The total length of Calreticulin/CALR Protein, Human (His) is 400 a.a., with molecular weight of ~50.6 kDa.
  • HY-P71420
    VCP Protein, Human (His)

    Transitional endoplasmic Reticulum ATPase; TER ATPase; 15S Mg(2+)-ATPase p97 Subunit; Valosin-Containing Protein; VCP

    		 Human E. coli
    VCP proteins are indispensable for Golgi stack dynamics, coordinating fragmentation during mitosis and postmitotic reorganization. It actively promotes the formation of the transitional endoplasmic reticulum (tER), enables ATP-dependent vesicle budding, and enables membrane transfer to the Golgi apparatus. VCP Protein, Human (His) is the recombinant human-derived VCP protein, expressed by E. coli , with C-6*His labeled tag. The total length of VCP Protein, Human (His) is 588 a.a., with molecular weight of ~75.0 kDa.
  • HY-P702352
    KDELR2 Protein, Mouse (Cell-Free, His)

    ER lumen protein-retaining receptor 2; KDEL endoplasmic reticulum protein retention receptor 2; KDEL receptor 2

    		 Mouse E. coli Cell-free
    KDELR2 Protein, a membrane receptor, crucially maintains endoplasmic reticulum (ER) resident proteins' localization. It binds the K-D-E-L sequence motif, retaining these proteins within the ER. This interaction facilitates vesicle-mediated recycling, ensuring proper subcellular localization through Golgi-to-ER protein return. KDELR2's pH-dependent binding, optimal at pH 5-5.4, underscores the regulatory role of pH in this vital cellular process. KDELR2 Protein, Mouse (Cell-Free, His) is the recombinant mouse-derived KDELR2 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of KDELR2 Protein, Mouse (Cell-Free, His) is 212 a.a., with molecular weight of 26.0 kDa.

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