GDF15 Mouse

Growth and Differentiation factor 15 Mouse Recombinant

Recombinant Mouse GDF15, produced in E. coli, is a single-chain polypeptide that lacks glycosylation. It consists of 138 amino acids (spanning positions 189 to 303), resulting in a molecular weight of 14.9 kDa. A 23-amino acid His-tag is attached to the N-terminus of GDF15 to facilitate purification using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT18129
Source
Escherichia Coli.
Appearance
A clear and sterile solution.

GDF3 Human

Growth Differentiation Factor-3 Human Recombinant

Recombinant human GDF3, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 124 amino acids with a molecular weight of 14.15 kDa. The protein is engineered with a 10 amino acid His tag at the N-terminus. Purification is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT18224
Source
Escherichia Coli.
Appearance
Sterile-filtered white powder, obtained through freeze-drying.

GDF5 Human

Growth Differentiation Factor-5 Human Recombinant

Recombinant Human Growth Differentiation Factor 5, expressed in E. coli, is a non-glycosylated homodimeric protein. Each subunit comprises 120 amino acids, resulting in a total molecular mass of 27.4 kDa. To facilitate bacterial expression, the N-terminal sequence has been modified by replacing the original Ala-Pro-Leu-Thr sequence with Lys. The protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18292
Source
Escherichia Coli.
Appearance
White, lyophilized powder, sterile-filtered.

GDF5 Human, His

Growth differentiation factor 5 Human Recombinant, His Tag

Recombinant Human GDF5, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 141 amino acids (382-501 a.a.). With a molecular weight of 15.8 kDa, this protein is fused to a 20 amino acid His Tag at its N-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18351
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

GDF5 Mouse

Growth and Differentiation factor 5 Mouse Recombinant

Recombinant Mouse GDF5, expressed in E. coli, is a non-glycosylated homodimeric protein. Each subunit, composed of 120 amino acids, contributes to a total molecular weight of 27.2 kDa. The protein is purified using proprietary chromatographic techniques, ensuring high purity for research applications.
Shipped with Ice Packs
Cat. No.
BT18414
Source
Escherichia Coli.
Appearance
The product appears as a sterile, white powder obtained through lyophilization (freeze-drying).

GDF5 Mouse, His

Growth differentiation factor 5 Mouse Recombinant, His Tag

Recombinant GDF5 Mouse, produced in E. coli, is a single, non-glycosylated polypeptide chain of 143 amino acids (376-495 a.a). With a molecular mass of 16 kDa, it comprises a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18491
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

GDF7 Human

Growth and Differentiation factor 7 Human Recombinant

Recombinant human GDF7, spanning amino acids 322 to 450, is produced in E. coli. This protein is a disulfide-linked homodimer, lacking glycosylation, and comprises a polypeptide chain of 129 amino acids. It has a molecular weight of 28 kDa. The purification of GDF-7 is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18552
Source
Escherichia Coli.
Appearance
The product appears as a white powder, obtained through sterile filtration and lyophilization (freeze-drying).

GDF7 Mouse

Growth and Differentiation factor 7 Mouse Recombinant

Recombinant Mouse GDF7, expressed in E. coli, is a non-glycosylated homodimeric protein. Each GDF7 molecule comprises two polypeptide chains, each containing 146 amino acids. The molecular weight of the dimer is 29.8 kDa. GDF-7 undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18623
Source
Escherichia Coli.
Appearance
Sterile, white powder obtained by lyophilization (freeze-drying).

BMP3 Human

Bone Morphogenetic protein-3 Human Recombinant

Recombinant Human BMP3, produced in E.coli, is a non-glycosylated, disulfide-linked homodimer. It comprises two chains, each containing 110 amino acids, resulting in a molecular mass of 24.8kDa. The purification of BMP-3 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT16993
Source
Escherichia Coli.
Appearance
The product appears as a sterile, filtered white powder that has been lyophilized (freeze-dried).

BMP4 Human, CHO

Bone Morphogenetic protein-4 Active Human Recombinant, CHO

Recombinant Human Bone Morphogenetic protein-4, produced in CHO cells, is a glycosylated homodimer chain comprising 2x116 amino acids. It has a total molecular mass of 26.2kDa. BMP4 undergoes purification using proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT17067
Source

CHO cells.

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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