Collagen I Antibody (YA5469)
(Synonyms: Collagen alpha-1; I; chain; Alpha-1 type I collagen; )Collagen I Antibody (YA5469) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Collagen I.
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Host:
Mouse
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Application:
ICC/IF, IHC-P
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|
| Dilution Ratio | 1:50-200 | 1:50-300 |
Product Details
Collagen I Antibody (YA5469) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Collagen I.
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Host Mouse
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 139 kDaNote: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
Synthetic Peptide of Collagen I
affinity chromatography.
Non-conjugated
Unmodified
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Collagen I is the predominant fibrillar collagen in the extracellular matrix and provides tensile strength, structural integrity, and mechanical support to bone, skin, tendon, ligament, and vascular tissues through the assembly of highly ordered collagen fibrils.[1][2] Type I collagen is composed of two α1 (I) chains and one α2 (I) chain that form a triple-helical procollagen molecule, which undergoes enzymatic processing and extracellular fibril formation to generate mature collagen fibers.[3][4] Mechanistically, collagen I regulates extracellular matrix organization and tissue architecture by forming stable cross-linked fibrillar networks that support cell adhesion, tissue repair, and connective tissue homeostasis.[1][3] In disease models, mutations affecting COL1A1 disrupt collagen assembly, fibrillogenesis, and matrix stability, leading to disorders including osteogenesis imperfecta and Ehlers-Danlos syndrome, highlighting the essential role of collagen I in skeletal and connective tissue integrity.[4] Compared with other collagen isoforms that form specialized extracellular matrix structures, collagen I is distinguished by its abundance and dominant contribution to fibrillar matrix formation in connective tissues.[1][2] For experimental applications, collagen I is widely used as a biomaterial and extracellular matrix model for investigating cell-matrix interactions, tissue remodeling, fibrosis, and regenerative processes because of its well-characterized fibrillar architecture and biomechanical properties.[1][2]
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Subcellular Localization
P08123: Secreted, extracellular space, extracellular matrix
P02452: Secreted, extracellular space, extracellular matrix -
Expression
Tissue_specificity: P08123: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite
P02452: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite -
Subunit
P08123: Trimers of one alpha 2 (I) and two alpha 1 (I) chains (Probable). Interacts (via C-terminus) with TMEM131 (via PapD-L domain) ; the interaction is direct and is involved in assembly and TRAPPIII ER-to-Golgi transport complex-dependent secretion of collagen (PubMed:32095531)
P02452: Interacts with TRAM2 (PubMed:14749390). -
Synonyms
Collagen alpha-1; I; chain; Alpha-1 type I collagen;
Documentation
References
[1]. Amirrah IN, et al. A Comprehensive Review on Collagen Type I Development of Biomaterials for Tissue Engineering: From Biosynthesis to Bioscaffold. Biomedicines. 2022 Sep 16;10(9):2307. [Content Brief]
[2]. Naomi R, et al. Current Insights into Collagen Type I. Polymers (Basel). 2021 Aug 9;13(16):2642. [Content Brief]