Collagen II Antibody - #AF5456

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Product: Collagen II Antibody
Catalog: AF5456
Description: Rabbit polyclonal antibody to Collagen II
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Bovine, Horse, Sheep, Rabbit, Chicken, Xenopus
Mol.Wt.: 141 kDa; 142kD(Calculated).
Uniprot: P02458
RRID: AB_2837940

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Related Downloads
MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

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:
Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Chicken(80%), Xenopus(90%)
Clonality:
Polyclonal
Specificity:
Collagen II Antibody detects endogenous levels of total Collagen II.
RRID:
AB_2837940
Cite Format: Affinity Biosciences Cat# AF5456, RRID:AB_2837940.
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 II collagen;Alpha-1 type II collagen;AOM;Cartilage collagen;Chondrocalcin;CO2A1_HUMAN;COL11A3;Col2a1;Collagen II alpha 1 polypeptide;SEDC;col 2;

Immunogens

Immunogen:
Uniprot:

P02458(CO2A1_HUMAN) >>Visit HPA database.

Gene(ID):
COL2A1(1280)
Expression:
P02458 CO2A1_HUMAN:

Isoform 2 is highly expressed in juvenile chondrocyte and low in fetal chondrocyte.

Description:
Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Sequence:
MIRLGAPQTLVLLTLLVAAVLRCQGQDVQEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASGQPGPKGQKGEPGDIKDIVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFAAQMAGGFDEKAGGAQLGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGANGIPGPIGPPGPRGRSGETGPAGPPGNPGPPGPPGPPGPGIDMSAFAGLGPREKGPDPLQYMRADQAAGGLRQHDAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPANVPKKNWWSSKSKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL

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
Bovine
100
Sheep
100
Rabbit
100
Xenopus
90
Chicken
80
Dog
56
Pig
0
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P02458 As Substrate

Site PTM Type Enzyme
Y41 Phosphorylation
K490 Ubiquitination
S536 Phosphorylation
K542 Acetylation
K764 Acetylation
K773 Acetylation
T1307 Phosphorylation
S1416 Phosphorylation

Research Backgrounds

Function:

Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.

PTMs:

The N-telopeptide is covalently linked to the helical COL2 region of alpha 1(IX), alpha 2(IX) and alpha 3(IX) chain. The C-telopeptide is covalently linked to an another site in the helical region of alpha 3(IX) COL2.

Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-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:

Isoform 2 is highly expressed in juvenile chondrocyte and low in fetal chondrocyte.

Subunit Structure:

Homotrimers of alpha 1(II) 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 (By similarity).

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: Viral > Human papillomavirus infection.

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

References

1). Naringenin protects against iron overload-induced osteoarthritis by suppressing oxidative stress. PHYTOMEDICINE, 2022 (PubMed: 35905566) [IF=7.9]
2). Vitamin K2 ameliorates osteoarthritis by suppressing ferroptosis and extracellular matrix degradation through activation GPX4's dual functions. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie, 2024 (PubMed: 38759289) [IF=7.5]

Application: WB    Species: Rat    Sample:

Fig. 8. GPX4 inhibitor RSL3 substantially attenuates VK2 protection of chondrocytes. (A-I) WB results for GPX4, NFκB, pMAPK/MAPK, Aggrecan, CollagenⅡ, SOX9, MMP3, MMP13 and Tubulin; (J) Quantitive analysis of relative Glutathione Peroxidase Activity; (K-L) GSH contents and ratio of GSH/GSSG; (M) Quantitative results of MDA content assay.
3). Oleic and linoleic acids promote chondrocyte apoptosis by inhibiting autophagy via downregulation of SIRT1/FOXO1 signaling. Biochimica et biophysica acta. Molecular basis of disease, 2024 (PubMed: 38378085) [IF=6.2]

Application: WB    Species: Rat    Sample:

Fig. 6. Regulation of the expression of extracellular matrix components in chondrocytes by SIRT1 and FOXO1. (A-E) Chondrocytes were transfected with siRNAs against FOXO1 and SIRT1 or with FOXO1- and SIRT1-expressing adenoviruses. (A) Western blot analysis of ADAMTS5, collagen II, and collagen X expression. (B) Quantitative analysis of the protein levels in (A) (n = 3). (C) Real-time PCR analysis of ADAMTS5, collagen II, and collagen X expression. (D) Confocal images of collagen II in chondrocytes (scale bar, 50 μm). (E) Fluorescence intensities of collagen II in (D). Error bars present mean ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.

Application: IF/ICC    Species: Rat    Sample:

Fig. 6. Regulation of the expression of extracellular matrix components in chondrocytes by SIRT1 and FOXO1. (A-E) Chondrocytes were transfected with siRNAs against FOXO1 and SIRT1 or with FOXO1- and SIRT1-expressing adenoviruses. (A) Western blot analysis of ADAMTS5, collagen II, and collagen X expression. (B) Quantitative analysis of the protein levels in (A) (n = 3). (C) Real-time PCR analysis of ADAMTS5, collagen II, and collagen X expression. (D) Confocal images of collagen II in chondrocytes (scale bar, 50 μm). (E) Fluorescence intensities of collagen II in (D). Error bars present mean ± SD. * p < 0.05, ** p < 0.01, and *** p < 0.001.
4). Recombinant human irisin regulated collagen II, matrix metalloproteinase‑13 and the Wnt/β‑catenin and NF‑κB signaling pathways in interleukin‑1β‑induced human SW1353 cells. Experimental and Therapeutic Medicine, 2020 (PubMed: 32256772) [IF=2.7]

Application: WB    Species: Human    Sample: SW1353 cells

Figure 2 Effect of irisin on MMP-13 and Col-II in IL-1β-induced SW1353 cells. SW1353 cells were treated with 20 mM irisin for 24 h, with or without 10 ng/ml IL-1β. (A) Col II protein levels, (B) MMP-13 protein levels, (C) Col II and MMP-13 protein expression, (D) Col II mRNA levels and (E) MMP-13 mRNA levels were evaluated by reverse transcription-quantitative PCR and western blot analysis (n=5/group). *P<0.05, **P<0.01 and ***P<0.001. IL-1β, interleukin-1β; MMP-13, matrix metalloproteinase-13; Col-II, collagen II; NC, negative control.

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