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Results for "

GRP

" in MedChemExpress (MCE) Product Catalog:

72

Inhibitors & Agonists

18

Peptides

1

Inhibitory Antibodies

7

Natural
Products

8

Recombinant Proteins

25

Isotope-Labeled Compounds

6

Antibodies

1

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Cat. No. Compare Product Name Species Source
  • HY-P70851
    LGALSL Protein, Human (His)

    Galectin-Related Protein; Lectin Galactoside-Binding-Like Protein; LGALSL; GRP; HSPC159

    		 Human E. coli
    The LGALSL protein was identified as a member of the galectin family, exhibits no affinity for lactose, and may not be involved in carbohydrate binding. This unique feature distinguishes LGALSL from typical galectins, which are known for their carbohydrate recognition domain and interaction with specific sugar moieties. LGALSL Protein, Human (His) is the recombinant human-derived LGALSL protein, expressed by E. coli , with C-6*His labeled tag. The total length of LGALSL Protein, Human (His) is 171 a.a., with molecular weight of ~18.0 kDa.
  • 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-P70944
    LSM4 Protein, Human (His)

    U6 snRNA-Associated Sm-Like Protein LSm4; Glycine-Rich Protein; GRP; LSM4

    		 Human E. coli
    The LSM4 protein plays a crucial role in pre-mRNA splicing, participating in the U4/U6-U5 tri-snRNP complex during spliceosome assembly, and as a component of the precatalytic spliceosome (spliceosome B complex). In the heptameric LSM2-8 complex, LSM4 specifically binds to the 3' U region of U6 snRNA. LSM4 Protein, Human (His) is the recombinant human-derived LSM4 protein, expressed by E. coli , with N-6*His labeled tag. The total length of LSM4 Protein, Human (His) is 139 a.a., with molecular weight of ~17.0 kDa.
  • HY-P700868
    GRP-10 Protein, Canine (HEK293, hFc)

    Gastrin-releasing peptide; GRP

    		 Canine HEK293
  • 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-P70943
    HYOU1 Protein, Human (HEK293, His)

    Hypoxia up-regulated protein 1; 150 kDa oxygen-regulated protein; ORP-150; 170 kDa glucose-regulated protein; GRP-170; HYOU1; ORP150

    		 Human HEK293
    The HYOU1 protein plays a crucial role in coordinating cytoprotective mechanisms in response to hypoxia, indicating its importance in cellular stress responses. It involves a potential molecular chaperone function and is actively involved in the protein folding process. HYOU1 Protein, Human (HEK293, His) is the recombinant human-derived HYOU1 protein, expressed by HEK293 , with C-10*His labeled tag. The total length of HYOU1 Protein, Human (HEK293, His) is 305 a.a., with molecular weight of 65-75 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.

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