Product: TIMP1 Antibody
Catalog: AF7007
Description: Rabbit polyclonal antibody to TIMP1
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Sheep, Dog
Mol.Wt.: 24kDa; 23kD(Calculated).
Uniprot: P01033
RRID: AB_2835315

View similar products>>

   Size Price Inventory
 50ul $250 In stock
 100ul $350 In stock
 200ul $450 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IF/ICC 1:100-1:500, 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(85%), Bovine(92%), Horse(92%), Sheep(92%), Dog(85%)
Clonality:
Polyclonal
Specificity:
TIMP1 Antibody detects endogenous levels of total TIMP1.
RRID:
AB_2835315
Cite Format: Affinity Biosciences Cat# AF7007, RRID:AB_2835315.
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

Clgi; Collagenase inhibitor; Collagenase inhibitor, Human; EPA; EPO; Erythroid Potentiating Activity; Erythroid-potentiating activity; Fibroblast collagenase inhibitor; FLJ90373; HCI; Human Collagenase Inhibitor; Metalloproteinase inhibitor 1; Metalloproteinase inhibitor 1 precursor; OTTHUMP00000023214; TIMP 1; TIMP; TIMP metallopeptidase inhibitor 1; TIMP-1; Timp1; TIMP1 protein; TIMP1_HUMAN; Tissue Inhibitor of Metalloproteinase 1; Tissue inhibitor of metalloproteinases 1; Tissue inhibitor of metalloproteinases; Ttissue inhibitor of metalloproteinase 1 erythroid potentiating activity collagenase inhibitor;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P01033 TIMP1_HUMAN:

Detected in rheumatoid synovial fluid (at protein level).

Description:
TIMP1 Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16.
Sequence:
MAPFEPLASGILLLLWLIAPSRACTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTLYQRYEIKMTKMYKGFQALGDAADIRFVYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTYTVGCEECTVFPCLSIPCKLQSGTHCLWTDQLLQGSEKGFQSRHLACLPREPGLCTWQSLRSQIA

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
92
Bovine
92
Sheep
92
Pig
85
Dog
85
Rabbit
77
Xenopus
0
Zebrafish
0
Chicken
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P01033 As Substrate

Site PTM Type Enzyme
K45 Ubiquitination
K70 Ubiquitination
S178 Phosphorylation
K180 Ubiquitination

Research Backgrounds

Function:

Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors.

PTMs:

The activity of TIMP1 is dependent on the presence of disulfide bonds.

N-glycosylated.

Subcellular Location:

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 rheumatoid synovial fluid (at protein level).

Subunit Structure:

Interacts with MMP1, MMP3, MMP10 and MMP13, but has only very low affinity for MMP14. Interacts with CD63; identified in a complex with CD63 and ITGB1.

Family&Domains:

Belongs to the protease inhibitor I35 (TIMP) family.

Research Fields

· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway.   (View pathway)

References

1). Autophagic-CTSB-inflammasome axis modulates hepatic stellate cells activation in arsenic-induced liver fibrosis. Chemosphere (PubMed: 31669990) [IF=8.8]

Application: WB    Species: rat    Sample: HSC-t6 cells

Fig,5| NaAsO2-induced activation of NLRP3 inflammasome and HSCs were mediated by cytoplasmic CTSB. (A-C) HSC-t6 cells were pretreated with or without CA-074 me for 2 h and then treated with NaAsO2 for 24 h. (A) The cytoplasmic and lysosomal CTSB was detected by IF. White arrows indicate positive staining (Images are shown at 20×10 magnification). (B, C) The expression level of NLRP3,caspase-1 p20, IL-1β, Collagen-Ⅰ, a-SMA, MMP-1, and TIMP-1 were determined by Western blot.

Application: WB    Species: rat    Sample: livers

Fig.2 NaAsO2 induced autophagy, activation of NLRP3 inflammasome and 662 hepatic stellate cell in vivo. (A) The expression level of LC3 and p62 in rat livers 663 following exposure to NaAsO2. The protein fraction was analyzed by Western blot. (B) 664 The expression level of cytoplasmic CTSB in rat livers following exposure to NaAsO2. 665 The protein fraction was analyzed by Western blot. (C) The expression level of NLRP3 inflammasome-associated proteins in rat livers following exposure to NaAsO2. 667 The protein fraction was analyzed by Western blot. (D) The expression level of 668 Collagen- , α-SMA, MMP-1, and TIMP-1in rat livers following exposure to NaAsO2. 669 The protein fraction was analyzed by Western blot. (E) α-SMA was detected by IF. 670 White arrows indicate positive staining. Values are mean ± SD, and n = 5. *p < 0.05, 671 **p < 0.01 compared with the control group; Scale bar = 100 µm

2). Quercetin induces MGMT+ glioblastoma cells apoptosis via dual inhibition of Wnt3a/β-Catenin and Akt/NF-κB signaling pathways. Phytomedicine (PubMed: 37451151) [IF=7.9]

3). Chrysin ameliorates synovitis and fibrosis of osteoarthritic fibroblast-like synoviocytes in rats through PERK/TXNIP/NLRP3 signaling. Frontiers in Pharmacology (PubMed: 37021049) [IF=5.6]

4). Phillygenin Inhibits TGF-β1-induced Hepatic Stellate Cell Activation and Inflammation: Regulation of the Bax/Bcl-2 and Wnt/β-catenin Pathways. Inflammation (PubMed: 38393550) [IF=5.1]

Application: WB    Species: Mouse    Sample: mHSC

Fig. 5 PHI inhibited TGF-β1-induced HSC activation in mHSCs and LX-2 cells. b Western blotting analyses of α-SMA, Collagen I, TIMP1, and MMP2 in mHSCs.

5). Transforming Growth Factor Beta 1 and p44/42 Expression in Cardinal Ligament Tissues of Patients with Pelvic Organ Prolapse. MEDICAL SCIENCE MONITOR (PubMed: 34176919) [IF=3.1]

Application: IHC    Species: Human    Sample: cardinal ligament tissues

Figure 6 Immunohistochemical staining for MMP9, TIMP1, and caspase 3 in the cardinal ligament. (A–F) Representative images showing that compared with the control group, the expression of MMP9 and caspase 3 was significantly higher and that of TIMP1 was significantly lower in the POP group. Quantitative analysis (G–I). * P<0.05. Magnification: 200× (A1–F1) and 400× (A2–F2). POP – pelvic organ prolapse; TGF-β1 – transforming growth factor beta 1.

6). Modulation of Bleomycin-induced Oxidative Stress and Pulmonary Fibrosis by Ginkgetin in Mice via AMPK. Current Molecular Pharmacology (PubMed: 35249515) [IF=2.7]

7). Forsythiaside A Regulates Activation of Hepatic Stellate Cells by Inhibiting NOX4-Dependent ROS. Oxidative Medicine and Cellular Longevity (PubMed: 35035671)

Application: WB    Species: Rat    Sample: HSCs

Figure 4 FA promoted collagen metabolism. (A-B) The expression of MMP-1 and TIMP-1 mRNA. (C-D) The expression of MMP-1 and TIMP-1 proteins. (E-G) The content of MMP-1 and TIMP-1 in medium supernatant. (H) The content of hydroxyproline. Data of three independent experiments were represented by mean ± S.D. ∗∗∗p <0.001 TGF-β1 vs control; ∗∗p <0.01 TGF-β1 vs control. ###p <0.001 TGF-β1 + FA vs TGF-β1;##p <0.01 TGF-β1 + FA vs TGF-β1; #p <0.05 TGF-β1 + FA vs TGF-β1.

8). Jinlian Xiaodu Decoction Protects against Bleomycin-Induced Pulmonary Fibrosis in Rats. Evidence-based Complementary and Alternative Medicine (PubMed: 35783517)

Application: WB    Species: Rat    Sample: pulmonary tissue

Figure 7 Effect of JXD on the cell apoptosis in pulmonary tissue of BLM-induced PF rats. (a) The apoptotic cells in pulmonary tissues were stained by tunel test kit and observed with a fluorescence microscope (magnification, 200×). (b) The quantitative result of TUNEL staining, n = 6. (c) The representative band of Western blot. (d)–(g) The quantitative result of Western blot, n = 3. Data were expressed as mean ± SD. ##P < 0.01 vs. control; ∗p < 0.05, ∗∗p < 0.01 vs. BLM.

9). α7nAChR Prevents Premature Cervical Ripening by Inducing M2 Macrophage Polarization and Myofibroblast Differentiation.

10). Lipopolysaccharide-induced premature cervical ripening and inflammation in pregnant mice can be alleviated by nicotine. Research Square

Restrictive clause

 

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.