Product: ADAMTS5 Antibody
Catalog: DF13268
Description: Rabbit polyclonal antibody to ADAMTS5
Application: WB IHC
Cited expt.: WB, IHC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 72 kd; 102kD(Calculated).
Uniprot: Q9UNA0
RRID: AB_2846287

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200
*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%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
ADAMTS5 Antibody detects endogenous levels of total ADAMTS5.
RRID:
AB_2846287
Cite Format: Affinity Biosciences Cat# DF13268, RRID:AB_2846287.
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

A disintegrin and metalloproteinase with thrombospondin motifs 11; A disintegrin and metalloproteinase with thrombospondin motifs 5; A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif 5; A disintegrin like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 5 (aggrecanase 2); A disintegrin-like and metalloprotease with thrombospondin type 1 motif, 5; A Disintigrin And Metalloproteinase with ThromboSpondin motif-5; ADAM metallopeptidase with thrombospondin type 1 motif 5; ADAM TS 11; ADAM TS 5; ADAM TS5; ADAM-TS 11; ADAM-TS 5; ADAM-TS5; ADAMTS 11; ADAMTS 5; ADAMTS-11; ADAMTS-5; ADAMTS11; ADAMTS11, formerly; Adamts5; ADMP 2; ADMP-2; ADMP2; Aggrecanase 2; Aggrecanase-2; ATS5_HUMAN; FLJ36738; Implantin; ThromboSpondin motif-5;

Immunogens

Immunogen:

A synthesized peptide derived from human ADAMTS5, corresponding to a region within the internal amino acids.

Uniprot:
Gene(ID):
Expression:
Q9UNA0 ATS5_HUMAN:

Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.

Sequence:
MLLGWASLLLCAFRLPLAAVGPAATPAQDKAGQPPTAAAAAQPRRRQGEEVQERAEPPGHPHPLAQRRRSKGLVQNIDQLYSGGGKVGYLVYAGGRRFLLDLERDGSVGIAGFVPAGGGTSAPWRHRSHCFYRGTVDGSPRSLAVFDLCGGLDGFFAVKHARYTLKPLLRGPWAEEEKGRVYGDGSARILHVYTREGFSFEALPPRASCETPASTPEAHEHAPAHSNPSGRAALASQLLDQSALSPAGGSGPQTWWRRRRRSISRARQVELLLVADASMARLYGRGLQHYLLTLASIANRLYSHASIENHIRLAVVKVVVLGDKDKSLEVSKNAATTLKNFCKWQHQHNQLGDDHEEHYDAAILFTREDLCGHHSCDTLGMADVGTICSPERSCAVIEDDGLHAAFTVAHEIGHLLGLSHDDSKFCEETFGSTEDKRLMSSILTSIDASKPWSKCTSATITEFLDDGHGNCLLDLPRKQILGPEELPGQTYDATQQCNLTFGPEYSVCPGMDVCARLWCAVVRQGQMVCLTKKLPAVEGTPCGKGRICLQGKCVDKTKKKYYSTSSHGNWGSWGSWGQCSRSCGGGVQFAYRHCNNPAPRNNGRYCTGKRAIYRSCSLMPCPPNGKSFRHEQCEAKNGYQSDAKGVKTFVEWVPKYAGVLPADVCKLTCRAKGTGYYVVFSPKVTDGTECRLYSNSVCVRGKCVRTGCDGIIGSKLQYDKCGVCGGDNSSCTKIVGTFNKKSKGYTDVVRIPEGATHIKVRQFKAKDQTRFTAYLALKKKNGEYLINGKYMISTSETIIDINGTVMNYSGWSHRDDFLHGMGYSATKEILIVQILATDPTKPLDVRYSFFVPKKSTPKVNSVTSHGSNKVGSHTSQPQWVTGPWLACSRTCDTGWHTRTVQCQDGNRKLAKGCPLSQRPSAFKQCLLKKC

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
Sheep
100
Dog
100
Xenopus
100
Chicken
100
Rabbit
100
Zebrafish
67
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

Research Backgrounds

Function:

Metalloproteinase that plays an important role in connective tissue organization, development, inflammation, arthritis, and cell migration. ADAMTS5 is an extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including aggrecan, versican, brevican and neurocan. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its versican remodeling properties. Participates in development of brown adipose tissue and browning of white adipose tissue. Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection.

PTMs:

The precursor is cleaved by furin and PCSK7 outside of the cell.

C- and O-glycosylated. O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation can mediate the efficient secretion of ADAMTS family members. Can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).

Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity).

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:

Expressed at low level in placenta primarily but also detected in heart and brain, cervix, uterus, bladder, esophagus, rib cartilage, chondroblastoma, fibrous tissue and a joint capsule from an arthritic patient.

Family&Domains:

The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

References

1). Bioengineered Versatile Heterojunctions as Stress Busters Targeting Matrix Degradation and Ferroptosis for Osteoarthritis Therapy. ADVANCED FUNCTIONAL MATERIALS, 2025 [IF=19.0]

2). Dual functions of microRNA-17 in maintaining cartilage homeostasis and protection against osteoarthritis. Nature Communications, 2022 (PubMed: 35508470) [IF=16.6]

Application: WB    Species: Mouse    Sample:

Fig. 2 miR-17 inhibits cartilage destruction by targeting multiple pathological catabolic factors. a Luciferase activity of 293 T cells co-transfected with dual-luciferase reporter constructs containing wild-type or mutated 3′-UTRs, as well as negative control (mimic NC) or miR-17 mimic. The data presented are mean percentage changes over mimic NC ± s.e.m. n = 6 biologically independent samples (NC + wt UTR, miR-17+wt UTR); n = 4 biologically independent samples (NC + mut UTR, miR-17 + mut UTR). b Mouse articular chondrocytes were transfected with miR-17 mimic (50 nM) or mimic NC and treated with or without IL-1β (5 ng/mL) for 24 h. The protein levels of catabolic and anabolic factors were determined by western blot followed by densitometry analysis. Blots are representative of three independent experiments. c, d qRT-PCR analysis of catabolic genes in knee cartilage (c), and representative images of IHC staining and quantification of MMP13+, ADAMTS5+ and NOS2+ cells in joint sections (d) of mice subjected to sham or DMM surgery and intra-articular injections of agomir-NC or agomir-17 (1.5 nmol) for 4 weeks, beginning at 4 weeks after surgery. n = 5 biologically independent samples per group in c. For MMP13 and ADAMTS5 staining, n = 4 mice (sham); n = 5 mice (DMM, DMM + agomir-17). For NOS2 staining, n = 4 mice per group. e, f qRT-PCR analysis of catabolic genes (e) and representative images of MMP13, ADAMTS5, and NOS2 immunostaining, and quantification of positive cells (f) from knee joints of cKO mice subjected to DMM surgery and intra-articular injection of agomir-NC, or agomir-17 (2 nmol). The injections were performed at 1 week after surgery and samples were collected at 2.5 weeks after surgery. n = 4 biologically independent samples per group in (e); n = 4 mice per group in (f). All scale bars, 100 μm. Data are presented as mean ± s.e.m. or boxplots (center line, median; box limits, 25 to 75th percentiles; whiskers, min to max), and dots represent individual mice or biologically independent samples. NS, not significant, *P < 0.05, **P < 0.01, and ***P < 0.001 in (a, c–f). *P < 0.05 versus control group, °P < 0.05 versus IL-1β + mimic NC in (b). Two-sided Student’s t test for (a); one-way ANOVA with Bonferroni’s test for (b–f). Exact P values in (b): *P = 0.0011, °P = 0.0205 (MMP3); *P <0.0001, °P = 0.0039 (MMP13); *P = 0.0015, °P = 0.0040 (ADAMTS5); *P = 0.0001, °P = 0.0013 (NOS2); *P = 0.0013, P > 0.9999 (SOX9); *P = 0.0001, P > 0.9999 (COL2A1). Source data are provided as a Source Data file.

Application: IHC    Species: Mouse    Sample:

Fig. 2 miR-17 inhibits cartilage destruction by targeting multiple pathological catabolic factors. a Luciferase activity of 293 T cells co-transfected with dual-luciferase reporter constructs containing wild-type or mutated 3′-UTRs, as well as negative control (mimic NC) or miR-17 mimic. The data presented are mean percentage changes over mimic NC ± s.e.m. n = 6 biologically independent samples (NC + wt UTR, miR-17+wt UTR); n = 4 biologically independent samples (NC + mut UTR, miR-17 + mut UTR). b Mouse articular chondrocytes were transfected with miR-17 mimic (50 nM) or mimic NC and treated with or without IL-1β (5 ng/mL) for 24 h. The protein levels of catabolic and anabolic factors were determined by western blot followed by densitometry analysis. Blots are representative of three independent experiments. c, d qRT-PCR analysis of catabolic genes in knee cartilage (c), and representative images of IHC staining and quantification of MMP13+, ADAMTS5+ and NOS2+ cells in joint sections (d) of mice subjected to sham or DMM surgery and intra-articular injections of agomir-NC or agomir-17 (1.5 nmol) for 4 weeks, beginning at 4 weeks after surgery. n = 5 biologically independent samples per group in c. For MMP13 and ADAMTS5 staining, n = 4 mice (sham); n = 5 mice (DMM, DMM + agomir-17). For NOS2 staining, n = 4 mice per group. e, f qRT-PCR analysis of catabolic genes (e) and representative images of MMP13, ADAMTS5, and NOS2 immunostaining, and quantification of positive cells (f) from knee joints of cKO mice subjected to DMM surgery and intra-articular injection of agomir-NC, or agomir-17 (2 nmol). The injections were performed at 1 week after surgery and samples were collected at 2.5 weeks after surgery. n = 4 biologically independent samples per group in (e); n = 4 mice per group in (f). All scale bars, 100 μm. Data are presented as mean ± s.e.m. or boxplots (center line, median; box limits, 25 to 75th percentiles; whiskers, min to max), and dots represent individual mice or biologically independent samples. NS, not significant, *P < 0.05, **P < 0.01, and ***P < 0.001 in (a, c–f). *P < 0.05 versus control group, °P < 0.05 versus IL-1β + mimic NC in (b). Two-sided Student’s t test for (a); one-way ANOVA with Bonferroni’s test for (b–f). Exact P values in (b): *P = 0.0011, °P = 0.0205 (MMP3); *P <0.0001, °P = 0.0039 (MMP13); *P = 0.0015, °P = 0.0040 (ADAMTS5); *P = 0.0001, °P = 0.0013 (NOS2); *P = 0.0013, P > 0.9999 (SOX9); *P = 0.0001, P > 0.9999 (COL2A1). Source data are provided as a Source Data file.

3). Sustained therapeutic effects of self-assembled hyaluronic acid nanoparticles loaded with α-Ketoglutarate in various osteoarthritis stages. Biomaterials, 2024 (PubMed: 39326362) [IF=12.8]

4). The deubiquitinase USP11 ameliorates intervertebral disc degeneration by regulating oxidative stress-induced ferroptosis via deubiquitinating and stabilizing Sirt3. Redox biology, 2023 (PubMed: 37099926) [IF=10.7]

5). Anti-Stress and Anti-ROS Effects of MnOx-Functionalized Thermosensitive Nanohydrogel Protect BMSCs for Intervertebral Disc Degeneration Repair. Advanced healthcare materials, 2024 (PubMed: 38738846) [IF=10.0]

6). Pentraxin 3 regulated by miR-224-5p modulates macrophage reprogramming and exacerbates osteoarthritis associated synovitis by targeting CD32. Cell Death & Disease, 2022 (PubMed: 35739102) [IF=8.1]

Application: IF/ICC    Species: Mouse    Sample:

Fig. 2 PTX3 accelerates synovitis, cartilage erosion, and exacerbates OA development in mice. A, B Safranin O/fast green staining and Osteoarthritis Research Society International (OARSI) grades of knee cartilage from DMM mice treated with vehicle, recombinant mouse PTX3 (rmPTX3), or PTX3 neutralizing antibody (PTX3-NAb) for 4 weeks and 8 weeks. Scale bar: 100 µm. C–F IF staining and quantification of ADATMS5 and MMP13 in knee cartilage of controls and DMM mice treated with vehicle, rmPTX3, or PTX3-NAb for 8 weeks. Scale bar: 50 µm. G IF staining and quantification of COL2 in knee cartilage of controls and DMM mice treated with rmPTX3 or PTX3-NAb for 8 weeks. Scale bar: 50 µm. H, I H&E and synovitis score of synovial tissues from DMM mice treated with vehicle, rmPTX3, or PTX3-NAb for 4 weeks and 8 weeks. Scale bar: 100 µm. *P 

7). TMF inhibits extracellular matrix degradation by regulating the C/EBPβ/ADAMTS5 signaling pathway in osteoarthritis. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie, 2024 (PubMed: 38554527) [IF=6.9]

Application: WB    Species: Human    Sample: C28/I2 cells

Fig. 4. Knockdown of FOXO3a compromised the inhibitory effects of TMF on C/EBPβ-mediated ECM degradation. (A–B) IHC assays were used to detect the altered expression of FOXO3a. (C–D) The protein expression of FOXO3a in shRNA-FOXO3a-infected C28/I2 cells was detected by western blotting assays. (E–K) Western blotting assays were used to detect the protein expression of Aggrecan, ADAMTS5, C/EBPβ, p-C/EBPβ, caspase3, cleaved-caspase3, and FOXO3a in LV-sh-FOXO3a-infected C28/I2 cells treated with IL-1β. (L-M) The apoptosis rate was determined by a flow cytometer.

8). Comparison of Curative Effect of Human Umbilical Cord-Derived Mesenchymal Stem Cells and Their Small Extracellular Vesicles in Treating Osteoarthritis. International journal of nanomedicine, 2021 (PubMed: 34938076) [IF=6.6]

Application: IHC    Species: Human    Sample:

Figure 4. Exploration of the effects of two treatments on cartilage matrix in vivo. (A and B) The immunohistochemical staining was performed to clarify the expression of Collagen II, MMP13 and ADAMTS5 in articulate (The magnification in A is 100×, scale bar = 100 μm; in B is 400×, scale bar = 20 μm;). (C) Statistical analysis of the percentage of pixels in the image or selection in three groups. Data are expressed as mean ±SEM. Different number of asterisk (*) show significant differences between groups. (*= P

9). Unveiling MiR-3085-3p as a modulator of cartilage degeneration in facet joint osteoarthritis: A novel therapeutic target. Journal of orthopaedic translation, 2025 (PubMed: 39895864) [IF=5.9]

10). Pharmacological network analysis of the functions and mechanism of kaempferol from Du Zhong in intervertebral disc degeneration (IDD). Journal of orthopaedic translation, 2023 (PubMed: 36909862) [IF=5.9]

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