Key Product Details

Species Reactivity

Validated:

Human, Mouse

Cited:

Human, Mouse, Rat, Bovine, Transgenic Mouse

Applications

Validated:

Immunohistochemistry, Blockade of Receptor-ligand Interaction

Cited:

Immunohistochemistry, Immunohistochemistry-Paraffin, Western Blot, Neutralization, Immunocytochemistry, Functional Assay

Label

Unconjugated

Antibody Source

Polyclonal Goat IgG
View all Gremlin Primary Antibodies »

Product Specifications

Immunogen

Mouse myeloma cell line NS0-derived recombinant mouse Gremlin
Lys25-Asp184
Accession # O70326

Specificity

Detects human and mouse Gremlin in direct ELISAs.

Clonality

Polyclonal

Host

Goat

Isotype

IgG

Endotoxin Level

<0.10 EU per 1 μg of the antibody by the LAL method.

Scientific Data Images for Human/Mouse Gremlin Antibody

Gremlin antibody in Human Breast Cancer Tissue by Immunohistochemistry (IHC-P).

Gremlin in Human Breast Cancer Tissue.

Gremlin was detected in immersion fixed paraffin-embedded sections of human breast cancer tissue using Goat Anti-Human/Mouse Gremlin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF956) at 3 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Goat IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC004). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.

Gremlin antibody in Embryonic Mouse Ribs by Immunohistochemistry (IHC-Fr).

Gremlin in Embryonic Mouse Ribs.

Gremlin was detected in immersion fixed frozen sections of embryonic mouse ribs (15 d.p.c.) using 15 µg/mL Goat Anti-Human/Mouse Gremlin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF956) overnight at 4 °C. Tissue was stained with the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). View our protocol for Chromogenic IHC Staining of Frozen Tissue Sections.

Detection of Gremlin by Immunohistochemistry

Detection of Gremlin by Immunohistochemistry

Inverse relationship between expression of Grem1 protein and pSmad1/5 staining in mouse intestine. Sequential FFPE sections (5 μm) of mouse intestine were stained for Grem1 (A) or pSmad1/5 (B) as described in Methods. (C) Positively stained cells (empty bars) or villi tips (filled bars) were quantified in the indicated regions using Image J and data were plotted as mean pixel intensity –/+ SEM (n = 3 mice, 3 independent regions of intestine quantified per mouse). *p< 0.05, ***p< 0.001 using two-way ANOVA and Bonferroni post hoc test. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31384391), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Gremlin by Immunohistochemistry

Detection of Gremlin by Immunohistochemistry

Distinct pattern of endogenous Grem1 expression in mouse colon. Sections (5 μm) from FFPE colon samples (n = 4) from wild-type or Grem1-/- mice were processed for in situ hybridisation (A left) and immunohistochemistry (A right; B.) as described in Methods. Positive Grem1 mRNA and protein staining was imaged using DAB (brown) and sections were counterstained using haematoxylin and imaged using PathXL. (A) Grem1 mRNA is visible as brown, punctate staining in the muscularis mucosa layer. Scale bars 100 μm. (B) Grem1 protein staining is evident as brown staining in the muscularis layer and the base of the colonic crypts (left; scale bar 100 μm). Grem1 protein staining in the musclaris layer as well as cells of the colonic crypt. CBCC, crypt base columnar cells; P, Paneth cells; TA, transit-amplifying cells. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31384391), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Gremlin by Western Blot

Detection of Gremlin by Western Blot

VEGFR2-MEK-ERK axis mediated the enhancement of FAO from Gremlin 1. (A). Cell viability assay of human intestinal fibroblast cells CCD-18Co and CCD-112Co cells treated with 200 ng/ml Gremlin 1 and Rapamycin (10 nM), LY3214996 (10 nM) or stattic (10 μM) for 24 h. (B). Immunoblotting analysis of VEGFR2-MEK-ERK signaling in human intestinal fibroblast cells CCD-18Co and CCD-112Co cells treated with 200 ng/ml Gremlin 1 and LY3214996 (10 nM) for 24 h. Actin acted as loading control and re-used for illustrative purposes. (C). Immunofluorescence staining of a-SMA in human intestinal fibroblast cells CCD-18Co and CCD-112Co cells treated with 200 ng/ml Gremlin 1 and LY3214996 (10 nM). (D). The intensity statistical results of a-SMA immunofluorescence staining from five random fields of slides. E. OCR measurement of CCD-18Co and CCD-112Co cells treated with 200 ng/ml Gremlin 1 and LY3214996 (10 nM) for 24 h. p values are derived from one-way ANOVA analysis. Dunnett’s test was used to analysis the difference between control group to the other groups. **p ≤ 0.01; ***p ≤ 0.001. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/33967807), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Gremlin by Western Blot

Detection of Gremlin by Western Blot

BMP2, TGF-beta 1 and BMP8A show different effects on the expressional induction of Nog, Grem1 and Grem2. C3H10T1/2 cells were treated with BMP2 (1 nM), TGF-beta 1 (0.3 nM), BMP2 plus with TGF-beta 1 or BMP8A (1 nM) for 24 h. The transcript levels (upper panel) and encoding protein amounts (lower panel) of Nog (A), Grem1 (B) and Grem2 (C) were then evaluated. beta -actin amounts served as loading controls in immunoblotting. D To explore how BMP8A induces Grem1 expression, cells were treated with BMP8A in the absence or presence of SB431542 (SB) or dorsomorphin (DM) as indicated. Quantification data are presented as means ± SEM. *P < 0.05, ***P < 0.001 compared to no-treatment control. # P < 0.001 compared between indicated groups Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/36443839), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Gremlin by Western Blot

Detection of Gremlin by Western Blot

BMP2, TGF-beta 1 and BMP8A show different effects on the expressional induction of Nog, Grem1 and Grem2. C3H10T1/2 cells were treated with BMP2 (1 nM), TGF-beta 1 (0.3 nM), BMP2 plus with TGF-beta 1 or BMP8A (1 nM) for 24 h. The transcript levels (upper panel) and encoding protein amounts (lower panel) of Nog (A), Grem1 (B) and Grem2 (C) were then evaluated. beta -actin amounts served as loading controls in immunoblotting. D To explore how BMP8A induces Grem1 expression, cells were treated with BMP8A in the absence or presence of SB431542 (SB) or dorsomorphin (DM) as indicated. Quantification data are presented as means ± SEM. *P < 0.05, ***P < 0.001 compared to no-treatment control. # P < 0.001 compared between indicated groups Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/36443839), licensed under a CC-BY license. Not internally tested by R&D Systems.

Applications for Human/Mouse Gremlin Antibody

Application
Recommended Usage

Blockade of Receptor-ligand Interaction

In a functional ELISA, 1-3 µg/mL of this antibody will block 50% of the binding of 100 ng/mL of Recombinant Human BMP-4 (Catalog # 314-BP) to immobilized Recombinant Mouse Gremlin (Catalog # 956-GR) coated at 5 µg/mL (100 µL/well).

Immunohistochemistry

3-15 µg/mL
Sample: Immersion fixed frozen sections of embryonic mouse ribs (15 d.p.c.), and immersion fixed paraffin-embedded sections of human breast cancer tissue

Reviewed Applications

Read 2 reviews rated 4 using AF956 in the following applications:

Formulation, Preparation, and Storage

Purification

Antigen Affinity-purified

Reconstitution

Reconstitute at 0.2 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration.

Formulation

Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Shipping

Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Gremlin

Gremlin was identified in a Xenopus expression-cloning screen as a dorsalizing factor that can induce a secondary axis. A rat homolog, called Drm, was identified as a cDNA that was downregulated in v-mos transfected cells. Gremlin/Drm belongs to the DAN family of secreted glycoproteins that are BMP antagonists. Other members of the family include: cerberus, Dante, PRDC, caronte and DAN. DAN family members share a cysteine-rich domain that is structurally related to the cysteine-knot motif found in TGF-beta superfamily ligands. In vitro, Gremlin/Drm binds BMP-4 and BMP-2 indicating that it might interfere with BMP signaling. Gremlin/Drm acts as a BMP-2/4 antagonist in a variety of tissues and developmental processes including: Xenopus animal cap explants, chick limb bud outgrowth and chondrogenesis, murine lung branching morphogenesis, and osteogenic differentiation of mouse myoblasts and bone marrow stromal cells. In addition, expression of Gremlin/Drm has been shown to be downregulated in a wide range of human cancer cell lines. Mouse, human, chick and Xenopus homologs of Gremlin share over 80% amino acid identity. It is likely that various DAN family members and other BMP antagonists including Noggin, Chordin, Follistatin and TSG can selectively antagonize the activities of different subsets of TGF-beta superfamily ligands.

References

  1. Hsu, D.R. et al. (1998) Mol. Cell 1:673.
  2. Merino, R. et al. (1999) Development 126:5515.
  3. Shi, W. et al. (2001) Am. J. Physiol. Lung Cell Mol. Physiol. 280:L1030.
  4. Topol, L.Z. et al. (2000) J. Biol. Chem. 275:8785.

Alternate Names

DAND2, DRM, GREM1

Entrez Gene IDs

26585 (Human); 23892 (Mouse)

Gene Symbol

GREM1

UniProt

O70326

Additional Gremlin Products

Product Documents for Human/Mouse Gremlin Antibody

Certificate of Analysis

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Product Specific Notices for Human/Mouse Gremlin Antibody

For research use only

Related Research Areas

BMP Family
Somite Markers

Citations for Human/Mouse Gremlin Antibody

Customer Reviews for Human/Mouse Gremlin Antibody (2)

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  • Mouse Gremlin Antibody
    Name: Ruchi Gupta
    Application: ELISA
    Sample Tested: Recombinant protein
    Species: Human
    Verified Customer | Posted 07/09/2018
    Human/Mouse Gremlin Antibody AF956
  • Name: Anonymous
    Application: Immunohistochemistry-Paraffin
    Sample Tested: See PMID 23832098
    Species: Rat
    Verified Customer | Posted 01/12/2015

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