BMP 2 Human, Monomer

Bone Morphogenetic Protein-2 Human Recombinant, Monomer

Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 115 amino acids (283-396) and having a molecular mass of 13009 Dalton.
The BMP-2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16256
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

BMP 2 Protein Human

Bone Morphogenetic Protein-2 Human Recombinant

Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated polypeptide chain containing 2x115 amino acids and having a molecular mass of 26kDa.
The BMP-2 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16329
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BMP 4 Human

Bone Morphogenetic Protein-4 Human Recombinant

Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa.
The BMP-4 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16424
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BMP 5 Human

Bone Morphogenetic protein-5 Human Recombinant

BMP-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (317-454 a.a.) and having a total molecular mass of 15.7 kDa.
BMP-5 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16477
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

BMP 7 Human

Bone Morphogenetic Protein-7 Human Recombinant

Bone Morphogenetic Protein-7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 139 amino acids and having a molecular mass of 15679.97 Dalton.
The BMP-7 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16549
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BMP 7 Human, HEK

Bone Morphogenetic protein-7 Human Recombinant, HEK

BMP-7 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 30-38kDa due to glycosylation.
The BMP7 corresponds to amino acid residues 315 to 431 of the full-length BMP-7 precursor and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16625
Source
HEK.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BMP 7 Human, His

Bone Morphogenetic Protein-7 Human Recombinant, His Tag

BMP7 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 148 amino acids (293-431) and having a molecular mass of 16.8 kDa.
The BMP-7 is fused to 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16711
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

BMP 7 Human, Plant

Bone Morphogenetic Protein-7 Human Recombinant, Plant

Bone Morphogenetic Protein-7 Human Recombinant produced in Plant is a monomeric, glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 16.5kDa, and fused to a 6xHis-tag at the N-terminus.
The BMP-7 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16814
Source
Nicotiana benthamiana.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BMP13 Human

Bone Morphogenetic protein-13 Human Recombinant

BMP13 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.1kDa.
The BMP-13 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16911
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BMP3 Human

Bone Morphogenetic protein-3 Human Recombinant

BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.
The BMP-3 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16993
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Definition and Classification

Bone Morphogenetic Proteins (BMPs) are a group of growth factors and cytokines that belong to the Transforming Growth Factor-Beta (TGF-β) superfamily . They were initially discovered for their ability to induce the formation of bone and cartilage. BMPs are pivotal morphogenetic signals that orchestrate tissue architecture throughout the body . There are over 20 different BMPs, each with specific roles in various biological processes .

Biological Properties

Key Biological Properties: BMPs are multifunctional growth factors involved in bone and cartilage development, embryogenesis, hematopoiesis, and neurogenesis . They stimulate the differentiation of mesenchymal stem cells into osteoblasts, which are essential for bone formation .

Expression Patterns and Tissue Distribution: BMPs are expressed in various tissues, including bone, cartilage, teeth, and kidneys . They are secreted glycoproteins that play crucial roles in developmental processes .

Biological Functions

Primary Biological Functions: BMPs are essential for bone and cartilage development. They induce the formation of bone and cartilage by promoting the differentiation of mesenchymal cells into osteoblasts . BMPs also play roles in cell migration, growth, and differentiation during embryogenesis .

Role in Immune Responses and Pathogen Recognition: BMPs modulate inflammation, angiogenesis, and immune responses, providing biological cues for tissue repair, protection, and regeneration .

Modes of Action

Mechanisms with Other Molecules and Cells: BMPs function by binding to specific receptors on cell surfaces, initiating signaling pathways that result in osteoblast differentiation . They interact with type II and type I serine-threonine kinase receptors and transduce signals through Smad and non-Smad signaling pathways .

Binding Partners and Downstream Signaling Cascades: BMPs bind to their receptors, leading to the phosphorylation of Smad proteins. These phosphorylated Smads form complexes with Smad4, translocate to the nucleus, and regulate the transcription of target genes .

Regulatory Mechanisms

Regulatory Mechanisms: BMP signaling is finely tuned by various mechanisms, including extracellular antagonists, BMP prodomains, and co-receptors . These regulatory mechanisms ensure precise control of BMP activity and signaling outcomes .

Transcriptional Regulation and Post-Translational Modifications: BMP ligands are processed from larger precursor forms by proteases, which cleave the prodomain region away from the functional mature domain . This processing is crucial for the activation and regulation of BMP signaling .

Applications

Biomedical Research: BMPs are extensively studied for their roles in bone and cartilage development, as well as their potential therapeutic applications .

Diagnostic Tools and Therapeutic Strategies: Recombinant human BMPs (rhBMPs) are used in orthopedic applications such as spinal fusions, nonunions, and oral surgery . BMP-2 and BMP-7 are FDA-approved for specific uses . BMPs are also being explored for their potential in treating chronic kidney disease and other conditions .

Role in the Life Cycle

Role Throughout the Life Cycle: BMPs play critical roles from embryonic development to aging and disease. During embryogenesis, BMPs are involved in the formation of bone, cartilage, and other tissues . In adults, BMPs contribute to bone homeostasis, repair, and regeneration . Dysregulation of BMP signaling is associated with various pathological conditions, including cancer and fibrosis .

BMPs are essential for maintaining bone health throughout life, ensuring proper bone remodeling and regeneration . They are also involved in the regulation of osteoclast and osteoblast activity, which is crucial for bone homeostasis .

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