Recombinant Human BMP-8a Protein

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity

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Recombinant Human BMP-8a Protein Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human BMP‑8a is present at 1 μg/mL, the concentration of recombinant human BMPR‑1A Fc Chimera that produces 50% of the optimal binding response is approximately 1.5‑6 μg/mL.
Source
E. coli-derived human BMP-8a protein
Ala264-His402 & Val265-His402
Accession #
N-terminal Sequence
Ala264 & Val265
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
BMP8B
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
15.8 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using
1073-BP in the following applications:

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 20 μg/mL in sterile 4 mM HCl containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human BMP-8a Protein

  • BMP-8a
  • bone morphogenetic protein 8a
  • Op2
  • Osteogenic Protein 2

Background

BMP-8, also known as osteogenic protein 2 (OP-2), was first isolated from a hippocampal library in a screen to identify relatives of BMP-7 (OP-1) (1). BMPs are a family of structurally and functionally related proteins and represent a subfamily of the transforming growth factor beta (TGF-beta ) superfamily. BMPs were originally identified as protein regulators of cartilage and bone formation. They have since been shown to be involved in embryogenesis and morphogenesis of various tissues and organs (2). BMPs play roles in regulating growth, differentiation, chemotaxis, and apoptosis of various cell types, including mesenchymal, epithelial, hematopoetic, and neuronal cells.

There exist two highly related and closely linked genes, designated BMP-8a and -8b in mice and humans. For humans, the protein products of these two genes share 98% amino acid (aa) sequence identity in their pro- and mature regions. However in the mouse, the two proteins share 89% and 76% aa sequence homology in their pro- and mature regions, respectively (3). Mature human BMP-8a shares 91% and 70% aa sequence identity with mouse BMP-8a and -8b, respectively. Human BMP‑8a is synthesized as a large precursor protein that is cleaved at a dibasic cleavage site (RTPR) between aa residues 263 and 264 to release a 139 aa carboxy‑terminal domain. Expression patterns of the BMP-8 genes indicate that they regulate aspects of cell proliferation and/or differentiation during spermatogenesis and formation of the placenta (3). BMP-8 is also highly expressed in osteosarcomas (4).

  1. Ozkaynak, E. et al. (1992) J. Biol. Chem. 267:25220.
  2. Canalis, E. et al. (2003) Endocrine Rev. 24:218.
  3. Zhao, G-Q. et al. (1996) Mech. Dev. 57:159.
  4. Sulzbacher, I. et al. (2002) J. Clin. Pathol. 55:381.

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Publications for BMP-8a (1073-BP)(6)

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 2 applications: Bioassay, cell culture.


Filter By Application
Bioassay
(5)
cell culture
(1)
All Applications
Filter By Species
Human
(5)
Mouse
(1)
All Species
Showing Publications 1 - 6 of 6.
Publications using 1073-BP Applications Species
D Jung, J Xiong, M Ye, X Qin, L Li, S Cheng, M Luo, J Peng, J Dong, F Tang, W Shen, MM Matzuk, K Kee In vitro differentiation of human embryonic stem cells into ovarian follicle-like cells Nat Commun, 2017;8(0):15680. 2017 [PMID: 28604658] (Bioassay, Human) Bioassay Human
Dominguez, Antonia, Chiang, H Rosari, Sukhwani, Meena, Orwig, Kyle E, Reijo Pera, Renee A Human germ cell formation in xenotransplants of induced pluripotent stem cells carrying X chromosome aneuploidies. Sci Rep, 2014;4(0):6432. 2014 [PMID: 25242416] (Bioassay, Human) Bioassay Human
Sharma A, Huard C, Vernochet C, Ziemek D, Knowlton K, Tyminski E, Paradis T, Zhang Y, Jones J, von Schack D, Brown C, Milos P, Coyle A, Tremblay F, Martinez R Brown fat determination and development from muscle precursor cells by novel action of bone morphogenetic protein 6. PLoS ONE, 2014;9(3):e92608. 2014 [PMID: 24658703] (Bioassay, Mouse) Bioassay Mouse
Goyal, Akshi, Chavez, Shawn L, Reijo Pera, Renee A Generation of human induced pluripotent stem cells using epigenetic regulators reveals a germ cell-like identity in partially reprogrammed colonies. PLoS ONE, 2013;8(12):e82838. 2013 [PMID: 24349377] (cell culture, Human) cell culture Human
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 Widespread potential for growth-factor-driven resistance to anticancer kinase inhibitors. Nature, 2012;487(7408):505-9. 2012 [PMID: 22763448] (Bioassay, Human) Bioassay Human
Geens M, Sermon KD Sertoli cell-conditioned medium induces germ cell differentiation in human embryonic stem cells. J. Assist. Reprod. Genet., 2011;0(0):. 2011 [PMID: 21318592] (Bioassay, Human) Bioassay Human

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Bioinformatics

Gene Symbol BMP8B
Uniprot