Animal-Free BMP-8a Protein, Human (His)
Based on 1 Customer Validation
BMP-8 is a pleiotropic ligand protein act as a reproductive system regulator, enriched in the ovary. BMP-8 is encoded by a pair of genes BMP8A and BMP8B, belonging to TNF-β family. BMP-8A activates the SMAD1/5/8 and the SMAD2/3 pathways in granulosa cells, to inhibit gonadotropin-induced progesterone production and steroidogenesis-related gene expression. BMP-8A also involves in Nrf2 phosphorylation in cancer cells to promote survival and drug resistance. BMP-8a Protein, Human is 402 a.a. with 2 glycosylation domains. Animal-Free BMP-8a Protein, Human (His) is a animal free recombinant human protein produced in E. coli cells, with 139 a.a. (A264-H402) and C-terminal His-tag.This product is for cell culture use only.
- Species: Human
- Source: E. coli
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Biological Activity
Description
BMP-8 is a pleiotropic ligand protein act as a reproductive system regulator, enriched in the ovary. BMP-8 is encoded by a pair of genes BMP8A and BMP8B, belonging to TNF-β family[1]. BMP-8A activates the SMAD1/5/8 and the SMAD2/3 pathways in granulosa cells, to inhibit gonadotropin-induced progesterone production and steroidogenesis-related gene expression[1]. BMP-8A also involves in Nrf2 phosphorylation in cancer cells to promote survival and drug resistance[2]. BMP-8a Protein, Human is 402 a.a. with 2 glycosylation domains. Animal-Free BMP-8a Protein, Human (His) is a animal free recombinant human protein produced in E. coli cells, with 139 a.a. (A264-H402) and C-terminal His-tag.This product is for cell culture use only.
Background
"BMP-8 is a pleiotropic ligand protein act as a reproductive system regulator. BMP-8 is encoded by a pair of genes, BMP8A and BMP8B, belonging to TNF-β family. GMP-8 initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Both BMP8A and BMP8B are enriched in the ovary and activate canonical BMP signaling in different cells, including spermatogonia, P19 and 293T cells[1]. BMP-8 is widely found in different animals, while the sequences of BMP-8A and BMP-8B in human are highly different from Mouse with similarities of 85.96% and 74.44%, respectively.
As for BMP8A, which is mainly secreted by granulosa cells within growing ovarian follicles. BMP8A encodes a secreted ligand of the TGF-β superfamily of proteins to bind various TGF-beta receptors, leading to recruitment and activation of SMAD family transcription factors and regulate gene expression. The encoded preproprotein is proteolytically processed to generate each subunit of the disulfide-linked homodimer[2]. BMP-8A protein activates the SMAD1/5/8 and the SMAD2/3 pathways in granulosa cells, to inhibit gonadotropin-induced progesterone production and steroidogenesis-related gene expression[1]. BMP8A protein plays a role in development of the reproductive system by sustaining spermatogenesis by activating both SMAD1/5/9 and SMAD2/3 in spermatogonia. BMP-8A protein also activates Nrf2 and Wnt pathways in clear cell renal cell carcinoma (ccRCC) to promote cell proliferation and inhibit apoptosis[2].
As for BMP8B, which protein is secreted by brown/beige adipocytes and enhances energy dissipation, serves as an interconnected regulator of neuro-vascular remodeling in AT and is potential targets in obesity[3]. BMP8B increases brown adipose tissue thermogenesis through both central and peripheral actions[4]. Thus BMP8B contributes to adrenergic-induced remodeling of the neuro-vascular network in adipose tissue, therefore through the adipocytes to 1) secrete neuregulin-4 (NRG4), which promotes sympathetic axon growth and branching in vitro, and 2) induce a pro-angiogenic transcriptional and secretory profile that promotes vascular sprouting[3]. BMP8B also involve in activation of caspase-3 and -9, and apoptosis to inhibit pancreatic cancer cell growth[5].
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In Vitro
BMP-8a (5 ng/mL; 6 d) can be used for hHEC lines differentiation accompanied with 5 ng/mL BMP-4[6].
BMP-8a (5 ng/mL; 6 d) can be used for PGCLC cells differentiation accompanied with 5 ng/mL BMP-4[7].
Verified Bioactivity
Measure by its ability to induce alkaline phosphatase production by ATDC5 cells. The ED50 for this effect is 10-19.4 ng/mL.
Technical Parameters
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Species Human
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Source E. coli
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Tag C-6*His
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Accession
AAP74559.1 (A264-H402)
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Molecular Construction
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N-term
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BMP-8a (A264-H402)
Accession # AAP74559.1 -
6*His
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C-term
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Protein Length
Full Length of Bone morphogenetic protein 8A Chain
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Synonyms
BMP8A; BMP-8A; Bone Morphogenetic Protein 8a; Bone Morphogenetic Protein 8A; OP-2; BMP8A Protein; Op2
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AA Sequence
AVRPLRRRQPKKSNELPQANRLPGIFDDVHGSHGRQVCRRHELYVSFQDLGWLDWVIAPQGYSAYYCEGECSFPLDSCMNATNHAILQSLVHLMKPNAVPKACCAPTKLSATSVLYYDSSNNVILRKHRNMVVKACGCH
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Predicted Molecular Mass
16.6 kDa
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Molecular Weight
Approximately 17 kDa, based on SDS-PAGE under reducing conditions.
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Purity
≥ 95%, as determined by reducing SDS-PAGE.
Product Properties
Lyophilized powder
1.Lyophilized from a 0.22 μm filtered solution of 20 mM sodium citrate, 0.2 M NaCl, pH 3.5, trehalose.
2.Lyophilized from a 0.22 μm filtered solution of 20 mM sodium citrate, 0.2 M NaCl, pH 4.5, trehalose.
3.Lyophilized from a 0.22 μm filtered solution of 20 mM sodium citrate, 0.2 M NaCl, pH 4.5.
Please refer to the lot-specific COA for specific buffer information.
<0.1 EU per 1 μg of the protein by the LAL method.
It is recommended to reconstitute to a concentration of 100-200 μg/mL in ddH2O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
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Data Sheet (265 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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Handling Instructions (2659 KB)
References
[1]. Wu FJ, et al. Human BMP8A suppresses luteinization of rat granulosa cells via the SMAD1/5/8 pathway. Reproduction. 2020 Mar;159(3):315-324. [Content Brief]
[2]. Yu YP, et al. BMP8A promotes survival and drug resistance via Nrf2/TRIM24 signaling pathway in clear cell renal cell carcinoma. Cancer Sci. 2020 May;111(5):1555-1566. [Content Brief]
[3]. Pellegrinelli V, et al. Adipocyte-secreted BMP8b mediates adrenergic-induced remodeling of the neuro-vascular network in adipose tissue. Nat Commun. 2018 Nov 26;9(1):4974. [Content Brief]
[4]. Whittle AJ, et al. BMP8B increases brown adipose tissue thermogenesis through both central and peripheral actions. Cell. 2012 May 11;149(4):871-85. [Content Brief]
[5]. Cheng Z, et al. BMP8B mediates the survival of pancreatic cancer cells and regulates the progression of pancreatic cancer. Oncol Rep. 2014 Nov;32(5):1861-6. [Content Brief]
[6]. Yan A, et al. DAZL regulates proliferation of human primordial germ cells by direct binding to precursor miRNAs and enhances DICER processing activity. Nucleic Acids Res. 2022 Oct 28;50(19):11255-11272. [Content Brief]
[7]. Hayashi K, et al. Stepwise differentiation from na茂ve state pluripotent stem cells to functional primordial germ cells through an epiblast-like state. Methods Mol Biol. 2013;1074:175-83. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)