Collagen III Antibody (YA6319)
(Synonyms: Collagen alpha-1(III) chain, COL3A1)Based on 1 Customer Validation
Collagen III Antibody (YA6319) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Collagen III.
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P, ICC/IF, IP, ELISA
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Conjugation:
Non-conjugated
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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IP
IP: Immunoprecipitation
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|---|---|---|---|---|---|
| Dilution Ratio | 1:20-100 | 1:1000-5000 | 1:200-1000 | 1:5000-20000 | 1:50-200 |
Product Details
Collagen III Antibody (YA6319) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Collagen III.
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Host Rabbit
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Clonality Monoclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 150 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.
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Calculated Molecular Weight Predicted band size: 138 kDa
Protein A
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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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.
Verification Images
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Western blot analysis was performed on protein extracts (25 μg) from HepG2 (lane 2), SH-SY5Y (lane 3), HeLa (lane 4), HT-1080 (lane 5), MCF-7 (lane 6), and A549 (lane 7) using Collagen III antibody. Proteins were transferred onto a 0.45 μm PVDF membrane using the Trans-Blot® Turbo™ system for 13 min. The membrane was then blocked with 5% nonfat milk in TBST (HY-K1025) for 1 h at room temperature. Thhe primary antibody (1:1000) and loading control antibody GAPDH Antibody (HRP) (HY-P80954A) (1:2500) were diluted in 5% nonfat milk in TBST and incubated with the membrane overnight at 4°C. After washing, the membrane of primary antibody was incubated with HRP-conjugated goat anti-rabbit IgG (H&L) secondary antibody (HY-P8001) (1:5000) diluted in 5% nonfat milk in TBST for 1 h at room temperature. Protein bands were visualized using an Ultra High Sensitivity ECL detection kit (HY-K1005).
Background
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Function
Collagen III (COL3A1) is a fibrillar extracellular matrix collagen synthesized as pre-procollagen and enriched in extensible tissues, including skin, blood vessels, intestine, uterus, and lung[1]. Mechanistically, collagen III regulates collagen I fibrillogenesis, fibril diameter, extracellular matrix architecture, and tissue mechanical integrity[2][3]. In wound models, collagen III supports re-epithelialization and limits scar-associated collagen fiber alignment, while reduced collagen III increases myofibroblast differentiation and scar deposition[4][5]. In disease models, COL3A1 mutations or deficiency produce vascular and dermal fragility resembling vascular Ehlers-Danlos syndrome[6][7]. Compared with collagen I, collagen III functions less as a dominant tensile scaffold and more as a fibril-network modifier that controls matrix organization, mechanosensing, and repair quality[2][3][4]. For experimental applications, the collagen III N-propeptide cysteine-rich domain attenuates TGFβ signaling and suppresses fibroblast activation, supporting its use as a mechanistic inhibitor tool in fibrosis and scarring studies[8].
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Subcellular Localization
Secreted, extracellular space, extracellular matrix
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Isoforms & Post-Translational Modification
P02461 has 2 isomers: P02461-1: 138564 Da (predicted); P02461-2: 111907 Da (predicted).
Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains;O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group -
Subunit
Trimers of identical alpha 1(III) chains. The chains are linked to each other by interchain disulfide bonds. Trimers are also cross-linked via hydroxylysines. Interacts with ADGRG1 (PubMed:28258187)
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SwissProt ID
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Synonyms
Collagen alpha-1(III) chain, COL3A1
Documentation
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Data Sheet (261 KB)
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SDS (251 KB)
- English - EN (251 KB)
- Français - FR (251 KB)
- Deutsch - DE (251 KB)
- Norwegian - NO (251 KB)
- Español - ES (251 KB)
- Swedish - SV (251 KB)
- Italian - IT (251 KB)
- Korean - KR (251 KB)
- Portuguese - PT (251 KB)
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User Guide for Antibodies (1077 KB)
References
[1]. Kuivaniemi H, et al. Type III collagen (COL3A1): Gene and protein structure, tissue distribution, and associated diseases. Gene. 2019 Jul 30;707:151-171. [Content Brief]
[2]. Liu X, et al. Type III collagen is crucial for collagen I fibrillogenesis and for normal cardiovascular development. Proc Natl Acad Sci U S A. 1997 Mar 4;94(5):1852-6. [Content Brief]
[3]. Wang C, et al. Type III collagen is a key regulator of the collagen fibrillar structure and biomechanics of articular cartilage and meniscus. Matrix Biol. 2020 Jan;85-86:47-67. [Content Brief]
[4]. Stewart DC, et al. Type III Collagen Regulates Matrix Architecture and Mechanosensing during Wound Healing. J Invest Dermatol. 2025 Apr;145(4):919-938.e14. [Content Brief]
[5]. Volk SW, et al. Diminished type III collagen promotes myofibroblast differentiation and increases scar deposition in cutaneous wound healing. Cells Tissues Organs. 2011;194(1):25-37. [Content Brief]
[6]. D'hondt S, et al. Type III collagen affects dermal and vascular collagen fibrillogenesis and tissue integrity in a mutant Col3a1 transgenic mouse model. Matrix Biol. 2018 Sep;70:72-83. [Content Brief]
[7]. Schwarze U, et al. Haploinsufficiency for one COL3A1 allele of type III procollagen results in a phenotype similar to the vascular form of Ehlers-Danlos syndrome, Ehlers-Danlos syndrome type IV. Am J Hum Genet. 2001 Nov;69(5):989-1001. [Content Brief]
[8]. Brisson BK, et al. Cysteine-rich domain of type III collagen N-propeptide inhibits fibroblast activation by attenuating TGFβ signaling. Matrix Biol. 2022 May;109:19-33. [Content Brief]