Recombinant Proteins
Product List
COL4A3 Human
Collagen Type IV Alpha 3 Human Recombinant
Human α3 chain of collagen IV; identical with the antigen called "glomerular basal membrane antigen" (GBM). Recombinant antigen for solid (ELISA) and fluid phase diagnostic assays. Calculated Molecular weight: 53kDa. Calculated isoelectric point: pH 8.9.
cDNA coding for a minicollagen version of the human collagen IV α3 chain fused to a hexa-histidine purification tag. The term minicollagen designates the removal of most of the epitope-less triplehelical collagenous region (situated between the N-terminal 7S domain and the C-terminal noncollagenous NC1 domain), which is a requirement for recombinant production of this antigen.
COL4A3 Human, Biotin
Collagen Type IV Alpha 3 Human Recombinant, Biotinylated
Human α3 chain of collagen IV; identical with the antigen called "glomerular basal membrane antigen" (GBM). Calculated Molecular weight: 48kDa. Calculated isoelectric point: pH 8.9. cDNA coding for a minicollagen version of the human collagen IV α3 chain fused to a 6-histidine purification tag. The term minicollagen designates the removal of most of the epitope-less triplehelical collagenous region (situated between the N-terminal 7S domain and the C-terminal noncollagenous NC1 domain), which is a requirement for recombinant production of this antigen.
COL4A3BP Human
Collagen Type IV Alpha 3 Binding Protein Human Recombinant
Collagen-I Bovine
Bovine Collagen-I
Bovine Collagen-I is a natural protein purified from bovine skin. Collagen-I is purified by proprietary chromatographic techniques.
Bovine skin.
Filtered White lyophilized (freeze-dried) powder.
Collagen-I Goat
Goat Collagen-I
Goat Collagen-I is a natural protein purified from Goat tissues. Collagen-I is purified by proprietary chromatographic techniques.
Goat tissues.
Filtered White lyophilized (freeze-dried) powder.
Collagen-I Mouse
Mouse Collagen-I
Mouse Collagen-I is a natural protein purified from Mouse tail tendon. Collagen-I is purified by proprietary chromatographic techniques.
Mouse tail tendon.
Filtered White lyophilized (freeze-dried) powder.
Collagen-II Bovine
Bovine Collagen-II
Bovine Collagen-II is a natural protein purified from bovine knee joint. Collagen-II is purified by proprietary chromatographic techniques.
Bovine knee joint.
Filtered White lyophilized (freeze-dried) powder.
Collagen-II Human
Human Collagen-II
Human Collagen-II is a natural protein purified from human cartilage. Collagen- II is purified by proprietary chromatographic techniques.
Human cartilage.
Filtered White lyophilized (freeze-dried) powder.
Collagen-III Bovine
Bovine Collagen-III
Mouse Collagen-III is a natural protein purified from washed dissected tissue into dilute acetic acid. Collagen-I is purified by proprietary chromatographic techniques.
Bovine washed dissected tissue.
Filtered White lyophilized (freeze-dried) powder.
Collagen-IV Bovine
Bovine Collagen-IV
Bovine Collagen-IV is a natural protein purified from bovine placenta. Collagen-IV is purified by proprietary chromatographic techniques.
Bovine placenta.
Filtered White lyophilized (freeze-dried) powder.
Introduction
Collagen is the most abundant protein in the human body, constituting about 25-35% of the total protein content. It is a key structural protein found in the extracellular matrix of various connective tissues, including skin, bones, tendons, ligaments, and cartilage . Collagen molecules are composed of three polypeptide chains that form a triple helix structure . There are at least 28 different types of collagen, classified based on their structure and function . The most common types include:
Collagen exhibits several key biological properties:
- Expression Patterns: Collagen is synthesized primarily by fibroblasts and other specialized cells such as osteoblasts and chondrocytes .
- Tissue Distribution: It is widely distributed across various tissues, providing structural integrity and mechanical strength. For instance, Type I collagen is abundant in skin and bones, while Type II is mainly found in cartilage .
- Hierarchical Structure: Collagen fibers are organized into fibrils, fibers, and bundles, each contributing to the unique mechanical properties of different tissues .
Collagen plays several crucial roles in the body:
- Structural Support: It provides tensile strength and structural integrity to tissues .
- Immune Responses: Collagen can influence immune responses by interacting with immune cells and modulating inflammation .
- Pathogen Recognition: Certain collagen types can bind to pathogens, aiding in their recognition and clearance by the immune system .
Collagen interacts with various molecules and cells through several mechanisms:
- Binding Partners: Collagen binds to cell surface receptors such as integrins and discoidin domain receptors (DDRs), initiating signaling cascades .
- Downstream Signaling: These interactions trigger downstream signaling pathways that regulate cell proliferation, differentiation, and migration .
- Enzymatic Breakdown: Enzymes like collagenases break down collagen, which is crucial for tissue remodeling and repair .
The expression and activity of collagen are tightly regulated:
- Transcriptional Regulation: Genes encoding collagen are regulated by transcription factors such as TGF-β and BMP1 .
- Post-Translational Modifications: Collagen undergoes several post-translational modifications, including hydroxylation and glycosylation, which are essential for its stability and function .
- Epigenetic Regulation: DNA methylation and histone modifications also play a role in regulating collagen gene expression .
Collagen has numerous applications in biomedical research and clinical practice:
- Biomedical Research: Collagen-based scaffolds are used in tissue engineering and regenerative medicine .
- Diagnostic Tools: Collagen biomarkers are used in diagnosing and monitoring diseases such as fibrosis and osteoarthritis .
- Therapeutic Strategies: Collagen is used in wound healing, drug delivery systems, and as a component of medical devices .
Collagen plays a vital role throughout the human life cycle:
- Development: During development, collagen provides the necessary framework for tissue formation and organ development .
- Aging: Collagen production decreases with age, leading to wrinkles, reduced skin elasticity, and weakened connective tissues .
- Disease: Alterations in collagen structure and function are associated with various diseases, including fibrosis, osteoarthritis, and certain cancers .
