BMPR1A Human

Bone Morphogenetic Protein Receptor Type IA Human Recombinant

BMPR1A Human Recombinant extracellular domain produced in baculovirus is a monomeric, glycosylated, Polypeptide chain fused with 6xHis tag at C-terminus and having a molecular mass of 23 kDa.
The BMR1A is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17258
Source
Insect Cells.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BMPR1A Human, CHO

Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO

Bone Morphogenetic Protein Receptor-1A Human Recombinant produced in CHO cells is a glycosylated homodimer chain containing 2x362 amino acids and having a total molecular mass of 80.8kDa.

BMPR1A is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT17341
Source

CHO cells.

Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BMPR1A Human, IgG-His

Bone Morphogenetic protein Receptor-1A Human Recombinant, IgG-His

BMPR1A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 371 amino acids (24-152a.a.) and having a molecular mass of 41.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
BMPR1A is fused with a 242 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT17460
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

BMPR1B Human

Bone Morphogenetic protein Receptor-1B Human Recombinant

BMPR1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (14-126 a.a) and having a molecular mass of 15.1kDa.
BMPR1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17531
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GDF10 Human

Growth differentiation factor 10 Human Recombinant

GDF10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (369-478 a.a.) and having a total molecular mass of 12.5 kDa.
GDF10 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17622
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GDF11 Human

Growth and Differentiation factor 11 Human Recombinant

GDF11 Human Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2x109 amino acids and having a total molecular mass of 24.9kDa. 

Shipped with Ice Packs
Cat. No.
BT17689
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

GDF11 Human, His

Growth and Differentiation factor 11 Human Recombinant, His Tag

GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa.
GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17734
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GDF15 D Human

Growth and Differentiation Factor 15 D-Variant Human Recombinant

GDF15 D-variant (His substitutes Asp at position 7) Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.5kDa.
The GDF15 D-variant is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17815
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

GDF15 Human

Growth and Differentiation Factor 15 Human Recombinant

GDF15 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, Polypeptide chain containing 2x113 amino acids and having a molecular mass of 24.8 kDa.
The GDF15 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17926
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

GDF15 Human, His

Growth and Differentiation Factor 15 Human Recombinant, His Tag

Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).
GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18043
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
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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