Product: Collagen III Antibody
Catalog: AF5457
Description: Rabbit polyclonal antibody to Collagen III
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 150-250 kDa; 139kD(Calculated).
Uniprot: P02461
RRID: AB_2837941

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:1000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(88%)
Clonality:
Polyclonal
Specificity:
Collagen III Antibody detects endogenous levels of total Collagen III.
RRID:
AB_2837941
Cite Format: Affinity Biosciences Cat# AF5457, RRID:AB_2837941.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Alpha 1 type III collagen; Alpha1 (III) collagen; CO3A1_HUMAN; COL 3A1; COL3A1; Collagen alpha 1(III) chain; Collagen alpha-1(III) chain; Collagen III alpha 1 chain precursor; Collagen III alpha 1 polypeptide; Collagen type III alpha 1 (Ehlers Danlos syndrome type IV autosomal dominant); Collagen type III alpha 1; Collagen type III alpha 1 chain; Collagen type III alpha; Collagen, fetal; EDS4A; Ehlers Danlos syndrome type IV, autosomal dominant; Fetal collagen; Type III collagen;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Description:
Defects in COL3A1 are a cause of Ehlers-Danlos syndrome type 3 (EDS3) [MIM:130020]; also known as benign hypermobility syndrome. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS3 is a form of Ehlers-Danlos syndrome characterized by marked joint hyperextensibility without skeletal deformity.
Sequence:
MMSFVQKGSWLLLALLHPTIILAQQEAVEGGCSHLGQSYADRDVWKPEPCQICVCDSGSVLCDDIICDDQELDCPNPEIPFGECCAVCPQPPTAPTRPPNGQGPQGPKGDPGPPGIPGRNGDPGIPGQPGSPGSPGPPGICESCPTGPQNYSPQYDSYDVKSGVAVGGLAGYPGPAGPPGPPGPPGTSGHPGSPGSPGYQGPPGEPGQAGPSGPPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGENGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSNGAPGQRGEPGPQGHAGAQGPPGPPGINGSPGGKGEMGPAGIPGAPGLMGARGPPGPAGANGAPGLRGGAGEPGKNGAKGEPGPRGERGEAGIPGVPGAKGEDGKDGSPGEPGANGLPGAAGERGAPGFRGPAGPNGIPGEKGPAGERGAPGPAGPRGAAGEPGRDGVPGGPGMRGMPGSPGGPGSDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPGGPGPQGPPGKNGETGPQGPPGPTGPGGDKGDTGPPGPQGLQGLPGTGGPPGENGKPGEPGPKGDAGAPGAPGGKGDAGAPGERGPPGLAGAPGLRGGAGPPGPEGGKGAAGPPGPPGAAGTPGLQGMPGERGGLGSPGPKGDKGEPGGPGADGVPGKDGPRGPTGPIGPPGPAGQPGDKGEGGAPGLPGIAGPRGSPGERGETGPPGPAGFPGAPGQNGEPGGKGERGAPGEKGEGGPPGVAGPPGGSGPAGPPGPQGVKGERGSPGGPGAAGFPGARGLPGPPGSNGNPGPPGPSGSPGKDGPPGPAGNTGAPGSPGVSGPKGDAGQPGEKGSPGAQGPPGAPGPLGIAGITGARGLAGPPGMPGPRGSPGPQGVKGESGKPGANGLSGERGPPGPQGLPGLAGTAGEPGRDGNPGSDGLPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPGPVGPAGKSGDRGESGPAGPAGAPGPAGSRGAPGPQGPRGDKGETGERGAAGIKGHRGFPGNPGAPGSPGPAGQQGAIGSPGPAGPRGPVGPSGPPGKDGTSGHPGPIGPPGPRGNRGERGSEGSPGHPGQPGPPGPPGAPGPCCGGVGAAAIAGIGGEKAGGFAPYYGDEPMDFKINTDEIMTSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKLDAIKVFCNMETGETCISANPLNVPRKHWWTDSSAEKKHVWFGESMDGGFQFSYGNPELPEDVLDVHLAFLRLLSSRASQNITYHCKNSIAYMDQASGNVKKALKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYRTRKAVRLPIVDIAPYDIGGPDQEFGVDVGPVCFL

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Horse
100
Sheep
100
Dog
100
Chicken
100
Rabbit
100
Xenopus
88
Bovine
78
Pig
75
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P02461 As Substrate

Site PTM Type Enzyme
S143 Phosphorylation
K757 Ubiquitination
S916 Phosphorylation
S1145 O-Glycosylation
Y1220 Phosphorylation
S1237 Phosphorylation
Y1370 Phosphorylation
Y1378 Phosphorylation
S1383 Phosphorylation
K1387 Acetylation

Research Backgrounds

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.

PTMs:

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.

Subcellular Location:

Secreted>Extracellular space>Extracellular matrix.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

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.

Family&Domains:

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function.

Belongs to the fibrillar collagen family.

Research Fields

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Organismal Systems > Immune system > Platelet activation.   (View pathway)

· Organismal Systems > Endocrine system > Relaxin signaling pathway.

· Organismal Systems > Digestive system > Protein digestion and absorption.

References

1). An asymmetric chitosan scaffold for tendon tissue engineering: In vitro and in vivo evaluation with rat tendon stem/progenitor cells. Acta Biomaterialia (PubMed: 29678676) [IF=9.7]

Application: IF/ICC    Species: rat    Sample: tendon

Fig. 6. | Analyses of tendon tissue by immunofluorescence. Fluorescence immunohistochemistry at the regenerated tendon in each group at 4 weeks. (A-D) The production of COL1; (E-H) The production of COL3; (I-L) The production of TNMD; (M-P) The production of CD31. Blue: DAPI (cell nuclei); Green:COL1/COL3/CD31; Red: TNMD. Scale bar = 100 μm.

Application: IHC    Species: rat    Sample: tendon

Fig. 5.| Detailed analyses of tendon tissue organization and immunohistochemistry. (A-E) DAPI staining and chart of calculated cell density. Data were mean ± S.D. * p < 0.05 vs. ED group. (F-Q)Representative images of regenerated tendon in each group at 4 weeks. Scale bar =100 μm.

2). Fisetin treatment alleviates kidney injury in mice with diabetes-exacerbated atherosclerosis through inhibiting CD36/fibrosis pathway. Acta Pharmacologica Sinica (PubMed: 37225845) [IF=8.2]

3). Protective role of Gentianella acuta on isoprenaline induced myocardial fibrosis in rats via inhibition of NF-κB pathway. BIOMEDICINE & PHARMACOTHERAPY (PubMed: 30554111) [IF=7.5]

4). Modified citrus pectin ameliorates myocardial fibrosis and inflammation via suppressing galectin-3 and TLR4/MyD88/NF-κB signaling pathway. Biomedicine & Pharmacotherapy (PubMed: 32172066) [IF=7.5]

Application: IHC    Species: rat    Sample: heart

Fig. 5. |Effects of MCP on ISO-induced myocardial fibrosis in rats. (A and B) Immunohistochemical analysis of collagen I and collagen Ⅲ protein in heart cross sections of different groups on day 15 and day 22 (200× magnification). Scale bars 100 μm.

Application: WB    Species: rat    Sample: heart

Fig. 6. |Effects of MCP on the expression of collagen Ⅰ and collagen Ⅲ induced by ISO in rats. Protein and mRNA levels of collagen Ⅰ and collagen Ⅲ were analyzed by western blot and qRT-PCR in each group on day 15 and day 22. (A) Protein expression of collagen Ⅰ and collagen Ⅲ were measured by western blot.

5). Corilagin alleviates hypertrophic scars via inhibiting the transforming growth factor (TGF)-β/Smad signal pathway. LIFE SCIENCES (PubMed: 33862115) [IF=6.1]

Application: WB    Species: Human    Sample: Hypertrophic scar tissue

Fig. 1. Corilagin downregulates mRNA and protein levels of collagen synthesis-related molecules in HSFs. A. Chemical structure of corilagin. B. Inhibitory effect of corilagin on COL1A1, COL1A2, COL3A1, and α-SMA mRNA expression level after HSFs were treated for 3 days. The expression levels were compared with that of GAPDH, n = 3. C. Protein levels of COL I, COL III, and α-SMA after corilagin application for 3 days by western blot analysis. The protein levels were compared with that of GAPDH. D. Quantification of protein levels detected by western blot analysis normalized to GAPDH level. n = 3. Data are shown as mean ± SD. *p < 0.05, **p < 0.01, ***p < 0.001. ns, no significance.

Application: WB    Species: human    Sample: HSFs

Fig. 1. |Corilagin downregulates mRNA and protein levels of collagen synthesis-related molecules in HSFs. C. Protein levels of COL I, COL III, and α-SMA after corilagin application for 3 days by western blot analysis. The protein levels were compared with that of GAPDH.

6). Daucosterol Alleviates Alcohol−Induced Hepatic Injury and Inflammation through P38/NF−κB/NLRP3 Inflammasome Pathway. Nutrients (PubMed: 36615880) [IF=5.9]

7). Exosomes derived from induced pluripotent stem cells suppresses M2-type macrophages during pulmonary fibrosis via miR-302a-3p/TET1 axis. International Immunopharmacology (PubMed: 34435585) [IF=5.6]

Application: WB    Species: mouse    Sample: lungs

Fig. 1.| Exosomes derived from iPSCs mitigated pulmonary fibrosis. Mice models of pulmonary fibrosis were established by intratracheal instillation with bleomycin and then treated with iPSC-exosomes or MEF-exosomes.The levels of TGF-β1, collagen I, and collagen III in the lungs were detected by western blot (D-E).

8). Bellidifolin Ameliorates Isoprenaline-Induced Myocardial Fibrosis by Regulating TGF-β1/Smads and p38 Signaling and Preventing NR4A1 Cytoplasmic Localization. Frontiers in Pharmacology (PubMed: 33995055) [IF=5.6]

9). Sodium butyrate ameliorates deoxycorticosterone acetate/salt-induced hypertension and renal damage by inhibiting the MR/SGK1 pathway. HYPERTENSION RESEARCH (PubMed: 32908237) [IF=5.4]

Application: WB    Species: rat    Sample: cortex and medulla

Fig. 2| Effects of NaBu on DOCA/salt-induced renal fibrosis and inflammation.a Representative Picrosirius red staining of collagen in kidney(n = 6 per group). Scale bar,100 μm. B Representative immunoblots of Col IA/Col IIIA/α-SMA and summarized intensities of blots in the cortex and medulla (n = 6–8 per group).

10). The aqueous extract of Gentianella acuta improves isoproterenol‑induced myocardial fibrosis via inhibition of the TGF‑β1/Smads signaling pathway. International Journal of Molecular Medicine (PubMed: 31939619) [IF=5.4]

Application: WB    Species: rat    Sample: heart

Figure 3. | G. acuta inhibits the expression of collagens I, III and α-SMA induced by ISO. (A) Immunohistochemical staining for collagens I, III and α-SMA,scale bars=100 µm. Bar graphs show the percentage of (B) collagens I, (C) III and (D) α-SMA. (E) Western blotting detection of collagens I, III and (F) α-SMA.

Application: IHC    Species: rat    Sample: heart

Figure 3. | G. acuta inhibits the expression of collagens I, III and α-SMA induced by ISO. (A) Immunohistochemical staining for collagens I, III and α-SMA,scale bars=100 µm. Bar graphs show the percentage of (B) collagens I, (C) III and (D) α-SMA. (E) Western blotting detection of collagens I, III and (F) α-SMA.

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