Collagen III Antibody (YA3616)(PBS only)
(Synonyms: EDS4A; EDSVASC; PMGEDSV)Collagen III Antibody (YA3616) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Collagen III.
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Host:
Mouse
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Isotype:
IgG
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Application:
IHC-P, FC, ELISA
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Reactivity :
Human
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Formulation:
Supplied in PBS, pH 7.4.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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FC
FC: Flow Cytometry
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|
| Dilution Ratio | 1:200-1:1000 | 1:200-1:400 | 1:10000 |
Product Details
Collagen III Antibody (YA3616) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Collagen III.
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Host Mouse
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 150 kDa
Note: 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: 139 kDa
Purified recombinant fragment of human COL3A1 (AA: 24-153) expressed in E. Coli.
affinity purified.
Non-conjugated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS, pH 7.4.
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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 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
EDS4A; EDSVASC; PMGEDSV
Documentation
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]
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