Zebrafish BMP2A (aa 272 - 386)

Name: Zebrafish BMP2A (aa 272 - 386)
SKU: DAG2585
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Zebrafish BMP2A (aa 272 - 386), recombinant protein from E. coli

COA

SDS

Datasheet

Summary

Product Overview

Recombinant Zebrafish BMP-2a was expressed in E. coli. Gln272-Arg386, with an N-terminal Met, Disulfide-linked homodimer (Accession # AAI63048.1)

Nature

Recombinant

Tag/Conjugate

Unconjugated

Purity

> 97%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Format

Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA with BSA as a carrier protein

Concentration

100 μg/mL

Buffer

4 mM HCl

Preservative

None

Storage

2-8°C short term, -20°C long term

Introduction

Bone morphogenetic protein 2 or BMP-2 belongs to the TGF-β superfamily of proteins. BMP-2 like other bone morphogenetic proteins, plays an important role in the development of bone and cartilage. It is involved in the hedgehog pathway, TGF beta signaling pathway, and in cytokine-cytokine receptor interaction. It is involved also in cardiac cell differentiation and epithelial to mesenchymal transition.

Antigen Description

BMP-2 is one of at least 20 structurally and functionally related BMPs, which are members of the transforming growth factor β (TGF-β) superfamily. BMPs were originally indentified as protein regulators of cartilage and bone formation. However, they are also involved in embryogenesis and morphogenesis of various tissues and organs. BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types, including mesenchymal cells, epithelial cells, hematopoietic cells, and neuronal cells. Similarly to other TGF-β family proteins, BMPs are highly conserved across animal species. At the amino acid sequence level, mature human, mouse, and rat BMP-2 are 100% identical, while mature human BMP-2 and zebrafish BMP-2a are 85% identical. Zebrafish have another homolog of BMP-2a, BMP-2b, which is 88% identical to BMP-2a in the mature region and corresponds to the swirl mutant. The combined expression pattern of zBMP-2a/2b/4 coincides with areas where BMP-2/4 expression would be found in other vertebrates. Biologically active BMP-2a is a disulfide-linked homodimer of the carboxy-terminal 115 amino acid residues that contains the characteristic seven conserved cysteine residues involved in the formation of the cysteine knot and the single interchain disulfide bond. Cellular responses to BMP-2a have been shown to be mediated by the formation of hetero-ogliomeric complexes of type I and type II serine/threonine kinase receptors. In contrast to the TGF-β type I receptor, which does not bind the ligand in the absence of the TGF-β receptor type II, both BMP receptor type I's can bind BMP-2 with high affinity in the absence of BMP receptor type II.

Keywords

BDA2; BMP 2; BMP 2A; BMP-2; BMP-2A; Bmp2; NBMP2A; Bone morphogenetic protein 2; Bone morphogenetic protein 2A; Zebrafish BMP-2 protein

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Documents

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References

Expression of C-terminal segments of bone morphogenetic protein in E-coli

ACTA BIOCHIMICA ET BIOPHYSICA SINICA

Authors: Lin, S; Xu, YK; Li, BL

Abstract

Two recombinant C-terminal segments of human bone morphogenetic protein 2A (BMP2A), designated as BMP23 (173aa) and BMP24 (134aa), mere expressed under the control of PL promoter in E. coli. SDS-PAGE analysis showed two induced protein bands at 20kD and 15.5kD, which were about 10% and 20% of the total bacterial protein, respectively. Both the expressed proteins were insoluble aggregates, which reached 80% purity after rapid preparation of the products as the inclusion body. The results of N-terminal amino acid sequencing showed that the first 15 amino acids at the N-terminal were identical to those encoded by the cDNA genes of both BMP23 and BMP24. After refolding botn BMP23 and BMP24 formed disulfide-linked dimeric protein bands in SDS-PAGE. Bioassay in vivo revealed that BMP23 induced chondrocytes differentiation and BMP24 stimulated collagen synthesis.

Conservation and divergence of Bmp2a, Bmp2b, and Bmp4 expression patterns within and between dentitions of teleost fishes

EVOLUTION & DEVELOPMENT

Authors: Wise, Sarah B.; Stock, David W.

Abstract

The diversity of tooth location in teleost fishes provides an excellent system for comparing genetic divergence between teeth in different species (phylogenetic homologs) with divergence between teeth within one species (iterative homologs). We have chosen to examine the expression of three members of the bone morphogenetic protein (Bmp) family because they are known to play multiple roles in tooth development and evolution in tetrapod vertebrates. We characterized expression of Bmp2a, Bmp2b, and Bmp4 during the development of oral and pharyngeal dentitions in three species of teleost fishes, the zebrafish (Danio rerio), Mexican tetra (Astyanax mexicanus), and Japanese medaka (Oryzias latipes). We found that expression in teleosts is generally highly conserved, with minor differences found among both iteratively homologous and phylogenetically homologous teeth. Expression of orthologous genes differs in several ways between the teeth of teleost fishes and those of the mouse, but between these vertebrate groups the summed expression pattern of Bmp genes is highly conserved. Significantly, the toothless oral region of the zebrafish lacks Bmp expression domains found in teleosts with oral teeth, implicating these genes in evolutionary tooth loss. We conclude that Bmp expression has been largely conserved in vertebrate tooth development over evolutionary time, and that loss of Bmp expression is correlated with region-specific loss of the dentition in a major group of fishes.

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