Product: Collagen I Antibody
Catalog: AF0134
Description: Rabbit polyclonal antibody to Collagen I
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Dog
Mol.Wt.: 129kDa; 139kD,129kD(Calculated).
Uniprot: P02452 | P08123
RRID: AB_2813771

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, 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:
Pig(100%), Bovine(100%), Horse(100%), Dog(100%)
Clonality:
Polyclonal
Specificity:
Collagen I Antibody detects endogenous levels of total Collagen I.
RRID:
AB_2813771
Cite Format: Affinity Biosciences Cat# AF0134, RRID:AB_2813771.
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 I collagen; Alpha 2 type I collagen; alpha 2 type I procollagen; alpha 2(I) procollagen; alpha 2(I)-collagen; Alpha-1 type I collagen; alpha1(I) procollagen; CO1A1_HUMAN; COL1A1; COL1A2; collagen alpha 1 chain type I; Collagen alpha-1(I) chain; collagen alpha-1(I) chain preproprotein; Collagen I alpha 1 polypeptide; Collagen I alpha 2 polypeptide; collagen of skin, tendon and bone, alpha-1 chain; collagen of skin, tendon and bone, alpha-2 chain; Collagen type I alpha 1; Collagen type I alpha 2; EDSC; OI1; OI2; OI3; OI4; pro-alpha-1 collagen type 1; type I proalpha 1; type I procollagen alpha 1 chain; Type I procollagen;

Immunogens

Immunogen:

A synthesized peptide derived from human Collagen I, corresponding to a region within N-terminal amino acids.

Uniprot:
Gene(ID):
Expression:
P02452 CO1A1_HUMAN:

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

P08123 CO1A2_HUMAN:

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Description:
This gene encodes one of the chains for type I collagen, the fibrillar collagen found in most connective tissues. Mutations in this gene are associated with osteogenesis imperfecta, Ehlers-Danlos syndrome, idiopathic osteoporosis, and atypical Marfan syndrome. Symptoms associated with mutations in this gene, however, tend to be less severe than mutations in the gene for alpha-1 type I collagen since alpha-2 is less abundant. Multiple messages for this gene result from multiple polyadenylation signals, a feature shared by most of the other collagen genes.
Sequence:
MFSFVDLRLLLLLAATALLTHGQEEGQVEGQDEDIPPITCVQNGLRYHDRDVWKPEPCRICVCDNGKVLCDDVICDETKNCPGAEVPEGECCPVCPDGSESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEAGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPGGPPGPKGNSGEPGAPGSKGDTGAKGEPGPVGVQGPPGPAGEEGKRGARGEPGPTGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGESGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGAKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPAGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGEKGSPGADGPAGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETGPAGPTGPVGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGPPGSPGEQGPSGASGPAGPRGPPGSAGAPGKDGLNGLPGPIGPPGPRGRTGDAGPVGPPGPPGPPGPPGPPSAGFDFSFLPQPPQEKAHDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQKNWYISKNPKDKRHVWFGESMTDGFQFEYGGQGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALLLQGSNEIEIRAEGNSRFTYSVTVDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPVCFL

MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEAGSAGPPGPPGLRGSPGSRGLPGADGRAGVMGPPGSRGASGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPPGPPGFQGLPGPSGPAGEVGKPGERGLHGEFGLPGPAGPRGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAVGTAGPSGPSGLPGERGAAGIPGGKGEKGEPGLRGEIGNPGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGAKGPKGENGVVGPTGPVGAAGPAGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRTGEVGAVGPPGFAGEKGPSGEAGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPAGKHGNRGETGPSGPVGPAGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKGHNGLQGLPGIAGHHGDQGAPGSVGPAGPRGPAGPSGPAGKDGRTGHPGTVGPAGIRGPQGHQGPAGPPGPPGPPGPPGVSGGGYDFGYDGDFYRADQPRSAPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRSSKDKKHVWLGETINAGSQFEYNVEGVTSKEMATQLAFMRLLANYASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFFVDIGPVCFK

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

PTMs - P02452/P08123 As Substrate

Site PTM Type Enzyme
K198 Acetylation
T209 Phosphorylation
S251 Phosphorylation
S389 Phosphorylation
S401 Phosphorylation
S404 Phosphorylation
S710 Phosphorylation
T981 Phosphorylation
K1064 Acetylation
T1073 Phosphorylation
S1104 Phosphorylation
S1124 Phosphorylation
T1138 O-Glycosylation
T1138 Phosphorylation
S1141 Phosphorylation
T1148 Phosphorylation
S1155 Phosphorylation
S1295 Phosphorylation

Research Backgrounds

Function:

Type I collagen is a member of group I collagen (fibrillar forming collagen).

PTMs:

Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.

Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.

O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.

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
Tissue Specificity:

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Subunit Structure:

Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 (By similarity). Interacts with TRAM2. Interacts with MFAP4 in a Ca (2+)-dependent manner (By similarity).

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 (By similarity).

Belongs to the fibrillar collagen family.

Function:

Type I collagen is a member of group I collagen (fibrillar forming collagen).

PTMs:

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

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
Tissue Specificity:

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Subunit Structure:

Trimers of one alpha 2(I) and two alpha 1(I) chains.

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

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.   (View pathway)

· Environmental Information Processing > Signaling molecules and interaction > ECM-receptor interaction.   (View pathway)

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· 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). 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.

2). Cyclic helix B peptide promotes random‐pattern skin flap survival via TFE3‐mediated enhancement of autophagy and reduction of ROS levels. British Journal of Pharmacology (PubMed: 34622942) [IF=7.3]

3). Targeting the Akt/PI3K/mTOR signaling pathway for complete eradication of keloid disease by sunitinib. Apoptosis (PubMed: 35802302) [IF=7.2]

4). Protein Expression Profile in Rat Silicosis Model Reveals Upregulation of PTPN2 and Its Inhibitory Effect on Epithelial-Mesenchymal Transition by Dephosphorylation of STAT3. International Journal of Molecular Sciences (PubMed: 32054021) [IF=5.6]

Application: WB    Species: mouse    Sample: MLE‐12 cells

Figure 6.|Effect of PTPN2 overexpression on SiO2 stimulated MLE‐12 cells.(A)Immunofluorescent staining for PTPN2 and E‐cad expression in NC‐LW299 and LW1049 cells with SiO2; Scale bars: 50μm. (B) Immunofluorescent staining for Vimentin expression in NC‐LW299 and LW1049 cells with SiO2; Scale bars: 50 μm. (C) Western blot for the expression levels of PTPN2, E‐cad, Vimentin, and p‐STAT3 in NC‐LW299 and LW1049 cells with SiO2

5). MiR-185-5p ameliorates endoplasmic reticulum stress and renal fibrosis by downregulation of ATF6. LABORATORY INVESTIGATION (PubMed: 32514126) [IF=5.0]

Application: WB    Species: human    Sample: HK2 cells

Fig. 3| MiR-185-5p prevents extracellular matrix accumulation and dedifferentiation of TGF-β1-induced HK2 cells by downregulating ATF6. a Expression of fibronectin, collagen I, and collagen III, and quantitative analysis of relative protein expression.

6). Down-regulation of miR-340-5p promoted osteogenic differentiation through regulation of runt-related transcription factor-2 (RUNX2) in MC3T3-E1 cells. Bioengineered (PubMed: 33818278) [IF=4.9]

Application: WB    Species: rat    Sample: femur tissues

Figure 1. The rat model of diabetic osteoporosis was established. (a-c) Diabetes was mediated by STZ in rats. Subsequently, bilateral OVX was carried out. The rats were fed for 8 weeks, and body weight was detected once a week. Then the animals were fasted overnight, and fasting blood glucose and blood insulin contents were assessed using the commercial kits. Finally, all the animals were sacrificed, and rat femur tissues were collected for following experiments. (d) Detection of BMD. (e) ALP staining was performed in femur tissues. Scale bar = 100 μm. (f) Measurement of miR-340-5p expression by qRT-PCR. (g) Evaluation of OCN, collagen-I, and RUNX2 levels with immunoblotting. β-actin was used as the internal reference. STZ, streptozotocin; OVX, ovariectomy; BMD, bone mineral density; ALP, alkaline phosphatase; OCN, osteocalcin. Data were expressed as means ± SD (N = 6 per group). # P < 0.05, ##P < 0.01, and ###P < 0.001 versus sham group; **P < 0.01 and ***P < 0.001 versus OVX group.

7). Danshensu alleviates bleomycin-induced pulmonary fibrosis by inhibiting lung fibroblast-to-myofibroblast transition via the MEK/ERK signaling pathway. Bioengineered (PubMed: 34187349) [IF=4.9]

Application: WB    Species: Mice    Sample: lung tissues

Figure 4. DSS inhibited fibroblast-myofibroblast differentiation via inhibiting the MEK/ERK signaling pathway in BLM-induced mice. (a) Immunohistochemistry analysis of FSP-1 and α-SMA in sections of lung tissues. Scale bar: 50 μm. (b, c) Protein expressions of α- SMA, COL-I, and TGF-β1 were detected by western blot. GAPDH was conducted as a loading control. (d, e) Protein expressions of p-MEK1/2, MEK1/2, p-ERK1/2, ERK1/2 were examined by western blot. GAPDH was conducted as a loading control. One-way ANOVA, *p < 0.05, ***p < 0.001, ****p < 0.0001

8). Rho GDP dissociation inhibitor α silencing attenuates silicosis by inhibiting RhoA/Rho kinase signalling. EXPERIMENTAL CELL RESEARCH (PubMed: 31029634) [IF=3.7]

Application: WB    Species: human    Sample: MRC-5 cells

Fig. 1. |Validation of RhoGDIα protein identified by 2-DE in MRC-5 cells. (A), Protein levels of pro COLI, α-SMA, and RhoGDIα in MRC-5 cells following TGF-β1 stimulation for 1 h, as analysed by western blotting (n = 3).

9). Euryachincoside, a novel phenolic glycoside with anti-hepatic fibrosis activity from Eurya chinensis. Planta Medica (PubMed: 35439837) [IF=2.7]

10). Calycosin attenuates pulmonary fibrosis by the epithelial-mesenchymal transition repression upon inhibiting the AKT/GSK3β/β-catenin signaling pathway. ACTA HISTOCHEMICA (PubMed: 34217047) [IF=2.5]

Application: WB    Species: Mice    Sample: lung tissues

Fig. 1. Calycosin prevented the pulmonary fibrosis induced by bleomycin in vivo. One day after 5 mg/kg BLM instillation, mice were orally administrated with 7 mg/kg or 14 mg/kg CA once a day for three weeks. (a) H&E stain- ing with injury score of lung tissues. Red arrow: edema and epithelial proliferation; Black arrow: inflammatory infiltration. Scale bar =100 μ m. (b) Masson trichrome staining with quantita- tive histological fibrosis scoring (Ashcroft score) of lung tissues. Blue: collagen fiber; Red: muscle fiber. Scale bar =100 μ m. (c) The con- tent of hydroxyproline in lung tissues. (d) The protein levels of collagen-I. (e-g) The concen- tration of TNF- α , IL-1β, and IL-6 in mice serum. Data were expressed as mean ± SD. n = 6 in each group. **p < 0.01 vs. control; #p < 0.05, ##p < 0.01 vs. BLM.

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