MMP13 Antibody - #DF6494

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Product: MMP13 Antibody
Catalog: DF6494
Description: Rabbit polyclonal antibody to MMP13
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 54kDa; 54kD(Calculated).
Uniprot: P45452
RRID: AB_2838456

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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
Clonality:
Polyclonal
Specificity:
MMP13 Antibody detects endogenous levels of total MMP13.
RRID:
AB_2838456
Cite Format: Affinity Biosciences Cat# DF6494, RRID:AB_2838456.
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

CLG 3; CLG3; Collagenase 3; Collagenase3; MANDP1; Matrix metallopeptidase 13 (collagenase 3); Matrix Metalloproteinase 13; Matrix metalloproteinase-13; MMP 13; MMP-13; Mmp13; MMP13_HUMAN;

Immunogens

Immunogen:
Uniprot:

P45452(MMP13_HUMAN) >>Visit HPA database.

Gene(ID):
MMP13(4322)
Expression:
P45452 MMP13_HUMAN:

Detected in fetal cartilage and calvaria, in chondrocytes of hypertrophic cartilage in vertebrae and in the dorsal end of ribs undergoing ossification, as well as in osteoblasts and periosteal cells below the inner periosteal region of ossified ribs. Detected in chondrocytes from in joint cartilage that have been treated with TNF and IL1B, but not in untreated chondrocytes. Detected in T lymphocytes. Detected in breast carcinoma tissue.

Description:
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]
Sequence:
MHPGVLAAFLFLSWTHCRALPLPSGGDEDDLSEEDLQFAERYLRSYYHPTNLAGILKENAASSMTERLREMQSFFGLEVTGKLDDNTLDVMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSHDLIFIFRGRKFWALNGYDILEGYPKKISELGLPKEVKKISAAVHFEDTGKTLLFSGNQVWRYDDTNHIMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPANSILWC

PTMs - P45452 As Substrate

Site PTM Type Enzyme
N117 N-Glycosylation
Y360 Phosphorylation
Y366 Phosphorylation

Research Backgrounds

Function:

Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.

PTMs:

The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro).

N-glycosylated.

Tyrosine phosphorylated by PKDCC/VLK.

Subcellular Location:

Secreted>Extracellular space>Extracellular matrix. Secreted.

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

Detected in fetal cartilage and calvaria, in chondrocytes of hypertrophic cartilage in vertebrae and in the dorsal end of ribs undergoing ossification, as well as in osteoblasts and periosteal cells below the inner periosteal region of ossified ribs. Detected in chondrocytes from in joint cartilage that have been treated with TNF and IL1B, but not in untreated chondrocytes. Detected in T lymphocytes. Detected in breast carcinoma tissue.

Subunit Structure:

Monomer. Interacts with TIMP1, TIMP2 and TIMP3. Binds (via the C-terminal region) to collagen.

Family&Domains:

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 (By similarity).

The C-terminal region binds to collagen.

Belongs to the peptidase M10A family.

Research Fields

· Organismal Systems > Immune system > IL-17 signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Relaxin signaling pathway.

References

1). Quercitrin alleviates cartilage extracellular matrix degradation and delays ACLT rat osteoarthritis development: an in vivo and in vitro study. Journal of Advanced Research (PubMed: 33364061) [IF=10.7]

Application: WB    Species: rat and human    Sample: rat chondrocytes and SW1353

Fig. 2. Quercitrin suppressed MMP13 expression and increased collagen Ⅱ deposition in IL-1b-induced rat chondrocytes and SW1353 cells. (A–D) Rat chondrocytes and SW1353 cells were pretreated with IL-1b (10 ng/ml) for 2 h prior to treatment with different concentrations of quercitrin (12.5, 25, and 50 lM) for 48 h. The cells were collected and collagen II and MMP13 mRNA expression levels were evaluated by RT-PCR. (E-J) Rat chondrocytes and SW1353 cells were pre-treated with IL-1b (10 ng/ml) for 2 h prior to treatment with different concentrations of quercitrin (12.5, 25, and 50 lM) for 48 h. The cells were collected and collagen II and MMP13 protein expression levels were evaluated by western blot. RT-PCR and western blot were repeated at least three times with similar results. All data are represented as the mean ± SD. *P < 0.05, **P < 0.01and ***P < 0.001 versus the control group; #P < 0.05, ##P < 0.01 and ###P < 0.001 versus the IL-1b-treated group. (K) Compared with control (n = 6), p110a mRNA expression levels were significantly decreased in severe OA patients (n = 12) by RT-PCR. ***P < 0.001 versus the control. Data from RT-PCR and western blot were analyzed by using one-way ANOVA, followed by Tukey’s range test.
2). Avicularin suppresses cartilage extracellular matrix degradation and inflammation via TRAF6/MAPK activation. PHYTOMEDICINE (PubMed: 34371251) [IF=7.9]

Application: WB    Species: Rat and human    Sample: chondrocytes

Fig. 2. Effects of avicularin on ECM degradation. (A-D) The mRNA levels of ACAN, Collagen 2, MMP3 and MMP13 in rat and human chondrocytes were detected by qPCR. The dates were shown as the means ± S.D. ** p < 0.01 and *** p < 0.001 compared with the control group; # p < 0.05, ## p < 0.01 and ### p < 0.001 compared with the IL-1β-induced group, n = 3. (E-F) The expression of MMP3, MMP13, ADAMTS5, SOX9, ACAN and Collagen II was detected by western blots.

Application: IHC    Species: Rat and human    Sample: chondrocytes

Fig. 7. Avicularin attenuates ECM degradation in ACLT rats. (A) ACAN, (B) Collagen II, (C) MMP3, (D) MMP13 and (E) TRAF6 immunohistochemistry of knee joint medial compartment cartilage. (F-J) Quantitative analysis of ACAN, Collagen II, MMP3, MMP13 and TRAF6. The values were shown as the means ± S.D. ** p < 0.01 and *** p < 0.001 compared with the control group; # p < 0.05, ## p < 0.01 and ### p < 0.001 compared with the ACLT group, n = 6. (K) The working model of how avicularin protects against OA development.
3). A network pharmacology strategy to investigate the anti-osteoarthritis mechanism of main lignans components of Schisandrae Fructus. International Immunopharmacology (PubMed: 34182246) [IF=5.6]

Application: WB    Species: Human    Sample: SW1353 cells

Fig. 6. (A) Analysis of the cytotoxicity induced by the 6 lignans in SW1353 cells. (B) Effects of the 6 lignans on collagen II gene expression in IL-1β- treated SW1353 cells. (C) Effects of the 6 lignans on MMP13 gene expression in IL-1β-treated SW1353 cells. (D) Effects of schisanhenol and gammaschisandrin on collagen II gene expression in IL-1β- treated SW1353 cells. (E) Effect of schisanhenol on MMP13 and collagen II protein expression in IL-1β- treated SW1353 cells. All the data are represented as the mean ± SD. Ns represents not significant, *p < 0.05, **p < 0.01 and ***p < 0.001, versus the control group; #p < 0.05, ##p < 0.01 and ###p < 0.001, versus the IL-1β-treated group.
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 (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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