COL1A2 Antibodies

Background

The COL1A2 gene encodes the α2 chain of type I collagen, an important fibrin that is widely present in the connective tissues of vertebrates. This gene product, by co-assembling with two other α1 chains, forms a triple helix structure, providing mechanical support and structural integrity for various tissues such as bones, skin, and tendons. Mutations in COL1A2 can disrupt the normal synthesis and assembly of collagen, leading to various hereditary connective tissue diseases such as osteogenesis imperfecia. Clinically, they are often manifested as fragile bones and loose joints. This gene was first identified in the late 1970s. The analysis of its sequence and structure has provided a key basis for understanding the formation mechanism of extracellular matrix and the molecular basis of related diseases. It remains an important research object in the fields of tissue engineering, genetic medicine and developmental biology to this day.

Structure Function Application Advantage Our Products

Structure of COL1A2

The COL1A2 gene encodes the α2 chain of type I collagen, a protein that is the main fibrin in connective tissues such as bones, skin, and tendons. Among different species, its molecular weight is approximately 130 kDa, and the specific value may fluctuate slightly due to the degree of post-translational modifications of the amino acid sequence (such as hydroxylation and glycosylation).

Species	Human	Mouse	Bovine	Rat
Molecular Weight (kDa)	About 130	About 130	About 129	About 130
Primary Structural Differences	The whole length is about 1366 amino acids	Conservative sequence is highly homologous, function	Collagen three screw area structure is extremely conservative	With the human proteins on the structure of domain are basically identical

This gene product does not exist alone in the body but is composed of two α1 chains (COL1A1) and one α2 chain (COL1A2) intertwined to form a unique three-strand helical structure, which is the basis for type I collagen to exert its powerful tensile strength. The core function of the COL1A2 protein is to provide mechanical support and structural framework for tissues. Gene mutations in this protein can disrupt the normal assembly of collagen fibers, leading to various genetic diseases such as osteogenesis imperfecia, which is characterized by fragile and easily broken bones. Therefore, this gene and its encoded protein are key molecular targets for studying the physiology and pathology of connective tissue and developing related diagnostic and therapeutic methods.

Fig. 1 Exon Map and Mutations of COL1A1/COL1A2 Genes and Their Protein Domains.¹

Key structural properties of COL1A2:

Characteristic triple helical structure
Rigid fiber assembly unit
Rely on post-translation embellishments

Functions of COL1A2

The main function of the type I collagen α2 chain encoded by the COL1A2 gene is to form the structural framework of connective tissue. However, it is also related to various pathological processes.

Function	Description
Structural support	As a major component of type I collagen, it provides tensile strength and mechanical stability for bones, skin, tendons, etc.
Extracellular matrix anchoring	Constitute the extracellular matrix network, provide attachment sites for cells, and participate in cell migration, differentiation and tissue repair.
Tissue development and remodeling	During embryonic development, bone growth, wound healing and tissue remodeling, its synthesis and degradation are precisely regulated.
Susceptibility to diseases	Mutations in the gene can disrupt the assembly of collagen fibers, leading to osteogenesis imperfectsis (brittle bone disease) and Ehlers-Danlos syndrome.
Signal transduction regulation	The complete collagen fiber network can bind and regulate the activity of various growth factors (such as TGF-β), indirectly affecting cell behavior.

The formation of the triple-helix structure of type I collagen is highly dependent on the precise stoichiometric ratio (1:2) of the products of the COL1A2 and COL1A1 genes. This imbalance in proportion or the replacement of a single amino acid (especially glycine residues) will directly disrupt the stability of the helix, causing the synthesized collagen to be unable to be secreted and assembled normally, thereby triggering genetic diseases with bone fragility as the core phenotype. Therefore, the functional integrity of this gene is crucial for maintaining the normal physiology of connective tissue.

Applications of COL1A2 and COL1A2 Antibody in Literature

1. Yuan, Xia, Yi He, and Wei Wang. "ceRNA network-regulated COL1A2 high expression correlates with poor prognosis and immune infiltration in colon adenocarcinoma." Scientific reports 13.1 (2023): 16932. https://doi.org/10.1038/s41598-023-43507-x

This study's analysis found that COL1A2 is highly expressed in colonic adenocarcinoma and indicates a poor prognosis. Its carcinogenic mechanism may be related to the regulation of the LINC00638/hsa-miR-552-3p axis and the remodeling of the tumor immune microenvironment, and it is a potential therapeutic target.

2. Bowers, Stephanie LK, et al. "Col1a2-Deleted mice have defective type I collagen and secondary reactive cardiac fibrosis with altered hypertrophic dynamics." Cells 12.17 (2023): 2174. https://doi.org/10.3390/cells12172174

In this study, through a gene-edited mouse model, it was found that although the deficiency of type I collagen (Col1a2) gradually causes myocardial fibrosis and dysfunction, acute inhibition of its production after injury can temporarily alleviate cardiac fibrosis and hypertrophy. The results show that type I collagen plays a dual role in cardiac homeostasis and injury repair.

3. Chen, Jing, et al. "Carrying both COL1A2 and FBN2 gene heterozygous mutations results in a severe skeletal clinical phenotype: an affected family." BMC Medical Genomics 15.1 (2022): 154. https://doi.org/10.1186/s12920-022-01296-8

This study has for the first time discovered that patients carrying both COL1A2 (p.Gly1102Arg) and FBN2 (p.Glu1370*) gene mutations have more severe abnormal bone phenotypes than those carrying only the COL1A2 mutation, suggesting that there may be a synergistic effect between the two genes.

4. Wang, Mingyuan, et al. "COL1A2 p. Gly1066Val variant identified in a Han Chinese family with osteogenesis imperfecta type I." Molecular Genetics & Genomic Medicine 7.5 (2019): e619. https://doi.org/10.1002/mgg3.619

In this study, a heterozygous missense mutation of c.3197G>T (p.Gly1066Val) in the COL1A2 gene was identified in a Han Chinese family with osteogenesis imperfecta type I. This mutation is co-isolated from the disease and may be a key pathogenic factor leading to abnormal collagen synthesis.

5. Wang, Ningqing, et al. "Regulation of COL1A2, AKT3 genes, and related signaling pathway in the pathology of congenital talipes equinovarus." Frontiers in Pediatrics 10 (2022): 890109. https://doi.org/10.3389/fped.2022.890109

This study, through sequencing and animal models, confirmed that the COL1A2 gene is upregulated in patients with congenital clubfoot and is involved in the disease occurrence together with the AKT3 gene and the PI3K-AKT3 signaling pathway, providing new ideas for mechanism research and prenatal diagnosis.

Creative Biolabs: COL1A2 Antibodies for Research

Creative Biolabs specializes in the production of high-quality COL1A2 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom COL1A2 Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our COL1A2 antibodies, custom preparations, or technical support, contact us at email.

Reference

Ho Duy, Binh, et al. "Mutation analysis of the COL1A1 and COL1A2 genes in Vietnamese patients with osteogenesis imperfecta." Human genomics 10.1 (2016): 27. https://doi.org/10.1186/s40246-016-0083-1