BMP6 Human

Bone Morphogenetic protein-6 Human Recombinant

Recombinant human BMP6, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 164 amino acids (375-513). With a molecular weight of 18 kDa, this protein comprises amino acids 375-513 of BMP6 and includes a 25 amino acid His-tag fused to its N-terminus. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17179
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

BMPR1A Human, IgG-His

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

Recombinant Human BMPR1A, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It comprises 371 amino acids (24-152a.a.), has a molecular weight of 41.4 kDa, and appears as a band at approximately 40-57 kDa on SDS-PAGE. The protein includes a C-terminal 242 amino acid hIgG-His tag and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17460
Source

Sf9, Baculovirus cells.

Appearance
A clear, colorless solution that has been sterilized by filtration.

BMPR1B Human

Bone Morphogenetic protein Receptor-1B Human Recombinant

Recombinant human BMPR1B, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 136 amino acids (residues 14-126) with a molecular weight of 15.1 kDa. This protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT17531
Source
Escherichia Coli.
Appearance
A clear, colorless, and sterile-filtered solution.

GDF10 Human

Growth differentiation factor 10 Human Recombinant

Recombinant human GDF10, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 111 amino acids (residues 369-478). With a molecular mass of 12.5 kDa, it encompasses the bioactive region of GDF10. The protein is purified using proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT17622
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

GDF11 Human

Growth and Differentiation factor 11 Human Recombinant

Recombinant human GDF11, produced in E. coli bacteria, is a non-glycosylated homodimer. Each GDF11 molecule consists of two identical chains, each containing 109 amino acids. The total molecular weight of the GDF11 homodimer is 24.9 kilodaltons (kDa).

Shipped with Ice Packs
Cat. No.
BT17689
Source
Escherichia Coli.
Appearance
White powder, sterile-filtered and freeze-dried.

GDF11 Human, His

Growth and Differentiation factor 11 Human Recombinant, His Tag

Recombinant human GDF11 protein, expressed in E. coli bacteria, is a single polypeptide chain without any sugar modifications. It consists of 132 amino acids (corresponding to positions 299-407a.a in the natural sequence) and has a molecular weight of 14.8 kilodaltons (kDa). For purification and detection purposes, a 23-amino acid His-tag is attached to the protein's N-terminus. The protein is purified using specialized chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT17734
Source
Escherichia Coli.
Appearance
Clear and colorless liquid, free from any particles or contamination.

GDF15 D Human

Growth and Differentiation Factor 15 D-Variant Human Recombinant

This product consists of recombinant human GDF15, specifically the D-variant where Asparagine at position 7 is replaced with Histidine. Produced in E. coli, this protein is a non-glycosylated homodimer, meaning it comprises two identical polypeptide chains, each containing 113 amino acids. The total molecular weight of the dimer is 24.5 kDa. Purification of the GDF15 D-variant is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT17815
Source
Escherichia Coli.
Appearance
The product appears as a sterile, white powder obtained through lyophilization (freeze-drying).

TSG Human

Twisted Gastrulation Protein Human Recombinant

Recombinant Human TWSG1 (26-223), produced in CHO cells, is a single, glycosylated polypeptide chain. It comprises 198 amino acids, with a molecular weight ranging from 35-43kDa as determined by SDS-PAGE. The variation in molecular weight is attributed to glycosylation. The purification of TWSG1 is carried out using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT18699
Source
CHO.
Appearance
White lyophilized (freeze-dried) powder, sterile and filtered.

BMP 7 Human

Bone Morphogenetic Protein-7 Human Recombinant

Recombinant Human Bone Morphogenetic Protein-7, produced in E. coli, is a monomeric, non-glycosylated polypeptide chain with a molecular weight of 15679.97 Daltons, comprising 139 amino acids. This protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT16549
Source
Escherichia Coli.
Appearance
White, sterile, lyophilized powder.

BMP 7 Human, HEK

Bone Morphogenetic protein-7 Human Recombinant, HEK

Recombinant Human BMP-7, produced in HEK cells, is a glycosylated homodimer linked by disulfide bonds. Its molecular weight varies between 30-38kDa due to glycosylation. This BMP-7 protein represents amino acids 315 to 431 of the full-length BMP-7 precursor and is purified using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16625
Source
HEK.
Appearance
White, lyophilized powder, sterile-filtered.
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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