Recombinant Human Gremlin Protein, CF

Catalog # Availability Size / Price Qty
5190-GR-050
Recombinant Human Gremlin Protein Bioactivity
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Product Details
Citations (17)
FAQs
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Reviews (2)

Recombinant Human Gremlin Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to inhibit alkaline phosphatase production by MC3T3‑E1 mouse preosteoblast cells. The ED50 for this effect is 0.025-0.15 μg/mL in the presence of 30 ng/mL of Recombinant Human BMP‑4 (Catalog # 314-BP).
Source
Mouse myeloma cell line, NS0-derived human Gremlin protein
Lys25-Asp184, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Analysis
Lys25
Structure / Form
Dimer
Predicted Molecular Mass
19.7 kDa
SDS-PAGE
25-30 kDa, under reducing conditions

Product Datasheets

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5190-GR

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

5190-GR

Formulation Lyophilized from a 0.2 μm filtered solution in PBS and EDTA.
Reconstitution Reconstitute at 200 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Scientific Data

Bioactivity Recombinant Human Gremlin Protein Bioactivity View Larger

Recombinant Human Gremlin (Catalog # 5190-GR) inhibits BMP-4-induced alkaline phosphatase production in the MC3T3-E1 mouse preosteoblast cell line. The ED50 for this effect is 0.025-0.15 µg/mL in the presence of 30 ng/mL of Recombinant Human BMP-4 (Catalog # 314-BP).

SDS-PAGE Recombinant Human Gremlin Protein SDS-PAGE View Larger

1 µg/lane of Recombinant Human Gremlin was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing major bands at 25‑30 kDa. Multiple bands in gel are due to variable glycosylation.

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Background: Gremlin

Gremlin, also known as Increased in High Glucose protein 2 (IHG-2) and Down-regulated in Mos-transformed cells protein (Drm), is a 28 kDa member of the Dan family of secreted glycoproteins (1-3). Human Gremlin is synthesized as a 184 amino acid (aa) precursor that contains a 24 aa signal sequence and a 160 aa mature region (SwissProt # O60565). The mature region contains one potential site for N-linked glycosylation (Asn 42), a cysteine-rich region, and a cysteine-knot motif (aa 94‑184) whose structure is shared by members of the TGF-beta superfamily (3). Post-translational modifications include glycosylation and phosphorylation (3). Gremlin exists in both secreted and membrane-associated forms (3). There are two isoforms for human Gremlin. Isoform 1 is the standard protein, and in isoform 2, there is a deletion of aa 39‑79. Human Gremlin shares 99% and 86% aa sequence identity with mouse and chick Gremlin, respectively. Northern blot analysis shows that Gremlin mRNA is highly expressed in the small intestine, fetal brain and colon, and weakly expressed in adult brain, ovary, prostate, pancreas and skeletal muscle (4). Gremlin functions as a bone morphogenetic protein (BMP) antagonist. It acts by binding to, and forming heterodimers with, BMP-2, BMP-4, and BMP-7, thus preventing them from interacting with their cell surface receptors (1). This mechanism is thought to be responsible for the pattern-inducing activity of Gremlin during embryonic development (5) and to play a role in human diseases, such as diabetic nephropathy (6). However, intracellular BMP-independent mechanisms of action (7) may mediate the ability of Gremlin to suppress transformation and tumorigenesis under certain experimental conditions (8-9). Gremlin also interacts with Slit proteins and acts as an inhibitor of monocyte chemotaxis (10). In addition, Gremlin has been found to be a proangiogenic factor expressed by endothelium (9).

References
  1. Hsu, D.R. et al. (1998) Mol. Cell 1:673.
  2. McMahon, R. et al. (2000) J. Biol. Chem. 275:9901.
  3. Wordinger, R.J. et al. (2008) Exp. Eye Res. 87:78.
  4. Topol, L.Z. et al. (2000) Cytogenet. Cell Genet. 89:79.
  5. Khokha, M.K. et al. (2003) Nat. Genet. 34:303.
  6. Lappin, D.W. et al. (2002) Nephrol. Dial. Transplant 17:65.
  7. Chen, B. et al. (2002) Biochem. Biophys. Res. Commun. 295:1135.
  8. Topol, L.Z. et al. (1997) Mol. Cell. Biol. 17:4801.
  9. Stabile, H. et al. (2007) Blood 109:1834.
  10. Chen, B. et al. (2004) J. Immunol. 173:5914.
Entrez Gene IDs
26585 (Human); 23892 (Mouse)
Alternate Names
Cell proliferation-inducing gene 2 protein; CKTSF1B1gremlin 1, cysteine knot superfamily, homolog; Cysteine knot superfamily 1, BMP antagonist 1gremlin 1, cysteine knot superfamily, homolog (Xenopus laevis); DAN domain family member 2; DAND2; DAND2GREMLIN; Down-regulated in Mos-transformed cells protein; DRM; DRMMGC126660; GREM1; gremlin 1; gremlin 1-like protein; Gremlin; gremlin-1; IHG-2; Increased in high glucose protein 2; increased in high glucose-2; proliferation-inducing gene 2

Citations for Recombinant Human Gremlin Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

17 Citations: Showing 1 - 10
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  1. alphaVbeta8 integrin targeting to prevent posterior capsular opacification (PCO)
    Authors: MH Shihan, SG Novo, Y Wang, D Sheppard, A Atakilit, TD Arnold, NM Rossi, AP Faranda, MK Duncan
    JCI Insight, 2021-11-08;0(0):.
    Species: Mouse
    Sample Types: In Vivo
    Applications: In Vivo
  2. Gremlin-1 Promotes Metastasis of Breast Cancer Cells by Activating STAT3-MMP13 Signaling Pathway
    Authors: NJ Sung, NH Kim, YJ Surh, SA Park
    International Journal of Molecular Sciences, 2020-12-03;21(23):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Cell Culture
  3. Gremlin-1 augments the oestrogen-related receptor alpha signalling through EGFR activation: implications for the progression of breast cancer
    Authors: SA Park, NJ Sung, BJ Choi, W Kim, SH Kim, YJ Surh
    Br. J. Cancer, 2020-06-23;0(0):.
    Species: Human
    Sample Types: Spheroid
    Applications: Cell Culture
  4. DHA inhibits Gremlin-1-induced epithelial-to-mesenchymal transition via ERK suppression in human breast cancer cells
    Authors: NJ Sung, NH Kim, NY Bae, HS Jo, SA Park
    Biosci. Rep., 2020-03-27;40(3):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Cell Culture
  5. ECHO, the executable CHOndrocyte: A computational model to study articular chondrocytes in healthy and disease
    Authors: S Schivo, S Khurana, K Govindaraj, J Scholma, J Kerkhofs, L Zhong, X Huang, J van de Pol, R Langerak, AJ van Wijnen, L Geris, M Karperien, JN Post
    Cell. Signal., 2019-12-11;0(0):109471.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. No evidence of Gremlin1-mediated activation of VEGFR2 signalling in endothelial cells
    Authors: LR Dutton, CL O' Neill, RJ Medina, DP Brazil
    J. Biol. Chem., 2019-10-11;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Cell Culture
  7. Targeting chemoresistant colorectal cancer via systemic administration of a BMP7 variant
    Authors: V Veschi, LR Mangiapane, A Nicotra, S Di Franco, E Scavo, T Apuzzo, DS Sardina, M Fiori, A Benfante, ML Colorito, G Cocorullo, F Giuliante, C Cipolla, G Pistone, MR Bongiorno, A Rizzo, CM Tate, X Wu, S Rowlinson, LF Stancato, M Todaro, R De Maria, G Stassi
    Oncogene, 2019-10-07;0(0):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  8. Cancer-associated fibroblast-derived Gremlin 1 promotes breast cancer progression
    Authors: J Ren, M Smid, J Iaria, DCF Salvatori, H van Dam, HJ Zhu, JWM Martens, P Ten Dijke
    Breast Cancer Res., 2019-09-18;21(1):109.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  9. Organoid culture media formulated with growth factors of defined cellular activity
    Authors: M Urbischek, H Rannikmae, T Foets, K Ravn, M Hyvönen, M de la Roch
    Sci Rep, 2019-04-17;9(1):6193.
    Species: Human, Mouse
    Sample Types: Whole Cells
    Applications: Bioassay
  10. Generation and Applications of a DNA Aptamer against Gremlin-1
    Authors: Q Li, Y Huo, Y Guo, X Zheng, W Sun, Z Hao
    Molecules, 2017-04-28;22(5):.
    Applications: Bioassay
  11. Diverse feather shape evolution enabled by coupling anisotropic signalling modules with self-organizing branching programme
    Authors: A Li, S Figueroa, TX Jiang, P Wu, R Widelitz, Q Nie, CM Chuong
    Nat Commun, 2017-01-20;8(0):ncomms14139.
    Species: Chicken
    Sample Types: In Vivo
    Applications: In Vivo
  12. Bone morphogenetic protein-9 suppresses growth of myeloma cells by signaling through ALK2 but is inhibited by endoglin.
    Authors: Olsen O, Wader K, Misund K, Vatsveen T, Ro T, Mylin A, Turesson I, Stordal B, Moen S, Standal T, Waage A, Sundan A, Holien T
    Blood Cancer J, 2014-03-21;4(0):e196.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  13. Interleukin-6 (IL-6) trans signaling drives a STAT3-dependent pathway that leads to hyperactive transforming growth factor-beta (TGF-beta) signaling promoting SMAD3 activation and fibrosis via Gremlin protein.
    Authors: O'Reilly S, Ciechomska M, Cant R, van Laar J
    J Biol Chem, 2014-02-18;289(14):9952-60.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  14. Quantitative kinetics analysis of BMP2 uptake into cells and its modulation by BMP antagonists.
    Authors: Alborzinia H, Schmidt-Glenewinkel H, Ilkavets I, Breitkopf-Heinlein K, Cheng X, Hortschansky P, Dooley S, Wolfl S
    J Cell Sci, 2012-10-17;126(0):117-27.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  15. Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors.
    Authors: Wilson TR, Fridlyand J, Yan Y, Penuel E, Burton L, Chan E, Peng J, Lin E, Wang Y, Sosman J, Ribas A, Li J, Moffat J, Sutherlin DP, Koeppen H, Merchant M, Neve R, Settleman J
    Nature, 2012-07-26;487(7408):505-9.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  16. Gremlin-1 induces BMP-independent tumor cell proliferation, migration, and invasion.
    Authors: Kim M, Yoon S, Lee S
    PLoS ONE, 2012-04-13;7(4):e35100.
    Species: Human
    Sample Types: Whole Cells
    Applications: Flow Cytometry
  17. Gremlin is a novel agonist of the major proangiogenic receptor VEGFR2.
    Authors: Mitola S, Ravelli C, Moroni E, Salvi V, Leali D, Ballmer-Hofer K, Zammataro L, Presta M
    Blood, 2010-07-21;116(18):3677-80.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance

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Reviews for Recombinant Human Gremlin Protein, CF

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Recombinant Human Gremlin Protein, CF
By Anonymous on 09/22/2018
Application: In vitro bioactivity in cell culture

Recombinant Human Gremlin Protein, CF
By Ruchi Gupta on 07/09/2018
Application: Gremlin ELISA