GDF15 Mouse

Growth and Differentiation factor 15 Mouse Recombinant

GDF15 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (189-303 a.a) and having a molecular mass of 14.9kDa.
GDF15 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18129
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GDF3 Human

Growth Differentiation Factor-3 Human Recombinant

GDF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a total molecular mass of 14.15 kDa.
GDF3 is fused to a 10 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18224
Source
Escherichia Coli.
Appearance
Filtered White lyophilized (freeze-dried) powder.

GDF5 Human

Growth Differentiation Factor-5 Human Recombinant

Growth Differentiation Factor 5 Human Recombinant produced in E.Coli is a homodimer, non-glycosylated polypeptide chain containing 2 x 120 amino acids and having a total molecular mass of 27.4kDa. To enable bacterial expression the N-terminal sequence of Ala-Pro-Leu-Thr was replaced with a Lys.
GDF5 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18292
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

GDF5 Human, His

Growth differentiation factor 5 Human Recombinant, His Tag

GDF5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (382-501 a.a.) and having a total molecular mass of 15.8 kDa.
GDF5 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT18351
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GDF5 Mouse

Growth and Differentiation factor 5 Mouse Recombinant

GDF5 Mouse 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 27.2kDa.
The GDF-5 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18414
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

GDF5 Mouse, His

Growth differentiation factor 5 Mouse Recombinant, His Tag

GDF5 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 143 amino acids (376-495 a.a) and having a molecular mass of 16kDa.
GDF5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18491
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

GDF7 Human

Growth and Differentiation factor 7 Human Recombinant

GDF7 Human Recombinant (322-450) produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 28kDa.
The GDF-7 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18552
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

GDF7 Mouse

Growth and Differentiation factor 7 Mouse Recombinant

GDF7 Mouse Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 146 amino acids and having a molecular mass of 29.8kDa.
The GDF-7 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18623
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

TSG Human

Twisted Gastrulation Protein Human Recombinant

TWSG1 Human Recombinant (26-223) produced in CHO is a single, glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass ranging from 35-43kDa on SDS-PAGE due to glycosylation.
The TWSG1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18699
Source
CHO.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

BMP 2 Human, HEK

Bone Morphogenetic protein-2 Human Recombinant, HEK

BMP-2 Human Recombinant produced in HEK cells is a glycosylated disulfide-linked homodimer, having a molecular weight range of 28kDa due to glycosylation. The BMP2 is purified by proprietary chromatographic techniques. 

Shipped with Ice Packs
Cat. No.
BT16163
Source
HEK.
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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