Abcam, ab88147, Anti-Collagen I antibody [3G3] - BSA and Azide free

Size: 100µg
Anti-Collagen I antibody [3G3] - BSA and Azide free (ab88147) is a mouse monoclonal antibody provided in a PBS only buffer for easy conjugation detecting Collagen I in Western Blot, IHC-P, ELISA . Suitable for Human, Mouse, . - BSA, sodium azide, and glycerol-free for easy conjugation - Over 70 publications - Trusted since 2009
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:3G3,
Isotype:IgG3,
Light chain type:kappa,
Carrier free:Yes,
Reacts with:Mouse, Human,
Applications:WB, IHC-P, ELISASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Recombinant Fragment Protein within Human COL1A1 aa 1000-1150. The exact immunogen used to generate this antibody is proprietary information.P02452,
Specificity:High levels of background are often observed when staining mouse tissue with mouse antibody. We would recommend ab270993 as an alternative for mouse samples.

Product details:
What is this antibody validated in?
Anti-Collagen I antibody [3G3] - BSA and Azide free (ab88147) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Immunohistochemistry (IHC-P), ELISA in Human, Mouse, samples.
What is the molecular weight of Collagen I?
Anti-Collagen I [3G3] - BSA and Azide free (ab88147) specifically detects a band for Collagen I (UniProt: P02452) at a molecular weight of 139kDa.
Trusted by the scientific community
Anti-Collagen I [3G3] - BSA and Azide free (ab88147) was first used in a scientific publication in 2009 and has been cited over 70 times in peer-reviewed journals.
Reviewed by scientists
Anti-Collagen I [3G3] - BSA and Azide free (ab88147) has over 10 independent reviews from customers.

Properties and Storage Information:
Form-Liquid, Purity-Tissue culture supernatant, Storage buffer-pH: 7.4Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Collagen type I also called collagen I is a structural protein expressed mainly in connective tissues such as skin tendon bone and ligaments. It serves as an important component in providing mechanical strength and integrity to these tissues. Collagen I is a fibrillar collagen known for its triple-helix structure composed of two alpha-1 chains and one alpha-2 chain and has a molecular mass of approximately 300 kDa. Researchers often employ collagen western blot and collagen ELISA techniques for its detection. Collagen suppliers offer various collagen antibodies used in these assays to study its distribution and function.
Biological function summary
Collagen type I plays a central role in maintaining the extracellular matrix and supporting cellular environments. It interacts with other matrix proteins and cells forming complexes that help in tissue development and repair. Type I collagen is especially important in bone matrix working alongside minerals like hydroxyapatite to provide rigidity and support. Anti-collagen antibodies aid in studying its biological functions and interactions which are critical to understanding tissue dynamics.
Pathways
Collagen type I interacts with multiple signaling cascades involved in tissue remodeling and repair. It is a significant player in the TGF-Β pathway which regulates fibrosis and wound healing processes. In these pathways proteins such as fibronectin and integrins work in concert with collagen type I to orchestrate cellular responses to damage. Researchers often examine its role in these pathways to uncover therapeutic possibilities for disease interventions.
Collagen type I has strong connections to conditions like osteogenesis imperfecta and fibrosis. Mutations or irregularities in collagen I production can lead to osteogenesis imperfecta a genetic disorder characterized by brittle bones. In fibrosis excessive collagen deposition disrupts normal tissue architecture contributing to organ dysfunction. In both conditions type I collagen interacts with other proteins like matrix metalloproteinases which modulate its breakdown and remodeling highlighting its importance in disease pathology.