Recombinant Human Chordin-Like 1 Protein Summary
Product Specifications
Glu22-Cys450, with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
1808-NR
Formulation | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein. |
Reconstitution | Reconstitute at 200 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin. |
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.
|
1808-NR/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. |
Reconstitution | Reconstitute at 200 μg/mL in sterile 4 mM HCl. |
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.
|
Reconstitution Calculator
Background: Chordin-like 1/CHRDL1
Chordin-like 1 (CHRDL1) also known as Chordin-like, ventroptin, and neuralin, is a secreted glycoprotein that has significant homology to chordin and acts as a bone morphogenetic protein (BMP) antagonist (1-3). Human Chordin-Like 1 cDNA encodes a 450 amino acid (aa) residue precursor protein with a putative 21 aa residue signal peptide. Chordin-Like 1 contains three internal cysteine-rich procollagen repeats (CRs) that are conserved in the spacing of their ten cysteines. The CRs of chordin, especially CR1 and CR3, have been shown to be the functional domains for BMP binding (1). The CR1 and CR3 of Chordin-Like 1 are most similar to CR3 of chordin (1). Chordin-Like 1 and chordin exhibit similar BMP inhibitory activity in vivo and directly interact with BMP-4 in vitro (1, 2). However, Chordin-Like 1 differs in its spatial and temporal expression from chordin. Mouse Chordin-Like 1 is detected in mesenchyme-derived cells such as the dermatome and limb bud, as well as chondrocytes of the developing skeleton later in development. In addition, Chordin-Like 1 is expressed embryonically in the gastrointestinal tract, kidney tubules, neural tube, CNS, cerebellum, derivatives of the neural crest cells, developing hair follicles, and the olfactory bulb where it is expressed in a gradient in the retina
(1-3). Chordin-Like 1 is also expressed in adult marrow stromal cells. Human CHRDL1 and the long form of mouse CHRDL1 share 93% aa sequence identity.
Multiple forms of human Chordin-Like 1 containing small deletions or insertions (including an E insertion between P94 and D95, a GKKAK deletion (aa residues
318-322), and/or another E insertion between K322 and E323) have been described. Similar isoforms have also been reported for mouse Chordin-Like 1. In addition, a short form of mouse Chordin-Like 1 with a shortened variant C-terminus but with all 3 CR domains intact also exists (1). These multiple forms were attributed to alternative splicing and transcriptional termination sites within the coding region of Chordin-Like 1.
- Nakayama, N. et al. (2001) Dev. Biol. 232:372.
- Sakuta, H. et al. (2001) Science 293:111.
- Coffinier, C. et al. (2001) Mech. Dev. 100:119.
Citations for Recombinant Human Chordin-Like 1 Protein
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.
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Citations: Showing 1 - 7
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Gradients of glucose metabolism regulate morphogen signalling required for specifying tonotopic organisation in the chicken cochlea
Authors: O'Sullivan, JDB;Blacker, TS;Scott, C;Chang, W;Ahmed, M;Yianni, V;Mann, ZF;
eLife
Species: Avian - Chicken
Sample Types: Whole Cells
Applications: Bioassay -
A gradient of Bmp7 specifies the tonotopic axis in the developing inner ear.
Authors: Mann Z, Thiede B, Chang W, Shin J, May-Simera H, Lovett M, Corwin J, Kelley M
Nat Commun, 2014-05-20;5(0):3839.
Species: Chicken
Sample Types: Whole Cells
Applications: Bioassay -
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 -
Inhibition of bone morphogenic protein 4 restores endothelial function in db/db diabetic mice.
Authors: Zhang Y, Liu J, Tian X, Wong W, Chen Y, Wang L, Luo J, Cheang W, Lau C, Kwan K, Wang N, Yao X, Huang Y
Arterioscler Thromb Vasc Biol, 2013-11-07;34(1):152-9.
Species: Mouse
Sample Types: Whole Tissue
Applications: Bioassay -
Bone morphogenetic protein-2/-4 upregulation promoted by endothelial cells in coculture enhances mouse embryoid body differentiation.
Authors: Talavera-Adame, Dodanim, Gupta, Ankur, Kurtovic, Silvia, Chaiboonma, Kira L, Arumugaswami, Vaithili, Dafoe, Donald C
Stem Cells Dev, 2013-09-24;22(24):3252-60.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
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 -
Chordin-like 1, a bone morphogenetic protein-4 antagonist, is upregulated by hypoxia in human retinal pericytes and plays a role in regulating angiogenesis.
Authors: Kane R, Godson C, O'Brien C
Mol. Vis., 2008-06-20;14(0):1138-48.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay
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