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AB7535

Native Human Collagen III protein

4

(3 Reviews)

|

(6 Publications)

Native Human Collagen III protein is a Human Full Length protein and suitable for ELISA, IP, SDS-PAGE and western blot. The predicted molecular weight of ab7535 native protein is 138 kDa

- Save time and ensure accurate results - use our Collagen III (COL3A1) protein as a control

View Alternative Names

Collagen alpha-1(III) chain, COL3A1

1 Images
SDS-PAGE - Native Human Collagen III protein (AB7535)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Native Human Collagen III protein (AB7535)

SDS-PAGE analysis of ab7535. Lane 1 : ab7535 Reduced 1 µg. Lane 2 : Pre-stained Molecular Weight Marker. Lane 3 : ab7535 Non-Reduced 1 µg.

Key facts

Expression system

Native

Tags

Tag free

Applications

IP, ELISA, WB, SDS-PAGE

applications

Biologically active

No

Accession

P02461

Animal free

No

Carrier free

No

Species

Human

Storage buffer

Preservative: 0.01% Sodium azide Constituents: 3% Acetic acid

storage-buffer

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Alternative Products

Proteins & Peptides

AB275791

Recombinant Human Collagen III protein (Tagged)

SDS-PAGE - Recombinant Human Collagen III protein (Tagged) (AB275791)

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  • 0

Complementary Products

Proteins & Peptides

AB314201

Native Bovine Collagen protein (FITC)

  • 0
  • 0
Proteins & Peptides

AB7536

Native Human Collagen IV protein

  • 3
  • 1
Primary Antibodies

AB184993

Anti-Collagen III antibody [EPR17673]

RabMAb|Recombinant|Lab Essentials

Immunocytochemistry/ Immunofluorescence - Anti-Collagen III antibody [EPR17673] (AB184993)

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  • 0
Secondary Antibodies

AB150077

Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488)

Immunocytochemistry/ Immunofluorescence - Goat Anti-Rabbit IgG H&L (Alexa Fluor® 488) (AB150077)

  • 5
  • 20
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1/10000", "notes":"<p></p>" }, "IP": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1/100 - 1/500", "notes":"<p>This product is not recommended for use under denaturing conditions in WB, IP, and ELISA. We would suggest testing it under native conditions.</p>" }, "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"1/1000", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Native","expressionSystem":null,"accessionNumber":"P02461","tags":[]}]
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Properties and storage information

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
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Collagen type III also known as COL3 and collagen III is a fibrillar protein with an approximate molecular mass of 138 kDa. This protein is a significant component of the extracellular matrix and is mainly expressed in connective tissues like skin lungs and vascular walls. You can also find it in developing tissues and fibrotic tissues reflecting its role during tissue growth and repair processes.
Biological function summary

Collagen type III contributes to maintaining the structural integrity of tissues. It forms a complex with collagen type I providing a scaffold that ensures mechanical strength and stability to tissues. This structural pairing of collagen type I and III highlights their cooperative function in supporting the extracellular matrix and regulating cell behavior in tissue repair and wound healing processes.

Pathways

Collagen type III is integral to the processes of tissue repair and fibrosis pathways. It interacts closely with proteins such as fibronectin and integrins contributing to the cellular adhesion and signaling pathways important for fibroblast function and migration. These interactions reflect its essential role in matrix assembly and stability influencing how cells respond to injury and repair damaged tissues.

Collagen type III mutations or dysregulation associate with vascular Ehlers-Danlos syndrome and keloids. In vascular Ehlers-Danlos syndrome defective collagen III compromises vessel wall integrity resulting in vascular fragility and rupture. In the context of keloids excessive collagen III accumulation in the skin illustrates its role in pathological fibrosis. Collagen type I is another protein that plays an important role in these conditions contributing along with collagen type III to the altered structural and functional properties observed in these disorders.
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Specifications

Form

Liquid

Additional notes

Human Collagen Type III has been prepared from human placenta and is chromatographically and immunologically pure. This product is free from other collagens, human serum proteins and non-collagen extracellular matrix proteins.

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General info

Function

Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12.

Sequence similarities

Belongs to the fibrillar collagen family.

Post-translational modifications

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.

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Product protocols

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Target data

Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12.
See full target information COL3A1
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Publications (6)

Recent publications for all applications. Explore the full list and refine your search

International journal of molecular sciences 24: PubMed37108227

2023

Autoreactivity against Denatured Type III Collagen Is Significantly Decreased in Serum from Patients with Cancer Compared to Healthy Controls.

Applications

Unspecified application

Species

Unspecified reactive species

Christina Jensen,Patryk Drobinski,Jeppe Thorlacius-Ussing,Morten A Karsdal,Anne-Christine Bay-Jensen,Nicholas Willumsen

Cancer biology & therapy 19:904-912 PubMed30067436

2018

A fragment of SPARC reflecting increased collagen affinity shows pathological relevance in lung cancer - implications of a new collagen chaperone function of SPARC.

Applications

Unspecified application

Species

Unspecified reactive species

S N Kehlet,T Manon-Jensen,S Sun,S Brix,D J Leeming,M A Karsdal,N Willumsen

Molecular medicine reports 18:3143-3152 PubMed30066869

2018

Extracellular matrix promotes proliferation, migration and adhesion of airway smooth muscle cells in a rat model of chronic obstructive pulmonary disease via upregulation of the PI3K/AKT signaling pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Zhengyan Wang,Rui Li,Rui Zhong

Experimental dermatology 27:973-980 PubMed29742305

2018

Red grape (Vitis vinifera L.) flavonoids down-regulate collagen type III expression after UV-A in primary human dermal blood endothelial cells.

Applications

Unspecified application

Species

Unspecified reactive species

Serena Di Francesco,Monica Savio,Nora Bloise,Giovanni Borroni,Lucia Anna Stivala,Riccardo G Borroni

Zoology (Jena, Germany) 118:147-60 PubMed25958104

2015

Ultrastructural and biochemical characterization of mechanically adaptable collagenous structures in the edible sea urchin Paracentrotus lividus.

Applications

Unspecified application

Species

Unspecified reactive species

Alice Barbaglio,Serena Tricarico,Ana R Ribeiro,Cristiano Di Benedetto,Marta Barbato,Desirèe Dessì,Valeria Fugnanesi,Stefano Magni,Fabio Mosca,Michela Sugni,Francesco Bonasoro,Mario A Barbosa,Iain C Wilkie,M Daniela Candia Carnevali

The British journal of dermatology 164:83-96 PubMed20849516

2010

Fibroblasts from the growing margin of keloid scars produce higher levels of collagen I and III compared with intralesional and extralesional sites: clinical implications for lesional site-directed therapy.

Applications

Unspecified application

Species

Unspecified reactive species

F Syed,E Ahmadi,S A Iqbal,S Singh,D A McGrouther,A Bayat
View all publications
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Product promise

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