TIMP2 Mouse mAb - Primary antibody, specific to TIMP2, Mouse IgG1

    Application:
  • Flow Cytometry
  • IF/ICC
  • IHC
  • WB
Features and benefits
  • Host species: Mouse
  • Species reactivity(Reacts with): Human,Mouse,Rat
  • Isotype: Mouse IgG1
  • Clone Number: 1554CT494.262.47
  • Conjugation: Unconjugated
Item Number
Ab131343
Grouped product items
SKUSizeAvailabilityPrice Qty
Ab131343-10μl
10μl
In stock
$66.90
Ab131343-50μl
50μl
In stock
$199.90
Ab131343-100μl
100μl
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$299.90
Ab131343-1ml
1ml
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$2,499.90

mAb (1554CT494.262.47); Mouse anti Human TIMP2 Antibody; WB, IHC, ICC, IF, Flow; Unconjugated

Basic Description

Product NameTIMP2 Mouse mAb - Primary antibody, specific to TIMP2, Mouse IgG1
SynonymsCSC 21K antibody | CSC-21K antibody | CSC21K antibody | Metalloproteinase inhibitor 2 antibody | Metalloproteinase inhibitor 2 precursor antibody | TIMP 2 antibody | TIMP metallopeptidase inhibitor 2 antibody | TIMP-2 antibody | TIMP2 antibody | TIMP2_HUM
Specifications & PurityExactAb™, Validated, Carrier Free, 0.5 mg/mL
Host speciesMouse
SpecificityTIMP2
ImmunogenRecombinant protein of human TIMP2 expressed in E.coli (AA 1-220).
Positive ControlWB: HeLa, A431, HUVEC and A549 cell lysates. IHC: Human kidney tissue. ICC/IF: A549 cells. Flow: K562 cells.
ConjugationUnconjugated
GradeCarrier Free, ExactAb™, Validated
Product Description

Mouse anti Human TIMP2 Antibody, Monoclonal (1554CT494.262.47), could be used for WB, IHC, ICC, IF, Flow and so on.
Application
WB: 1/2000
IHC: 1/200
IF: 1/25
Flow: 1/25
Protein Function
Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

Product Properties

IsotypeMouse IgG1
Light Chain Typekappa
SDS-PAGE150 kDa
Purification MethodProtein G purified
FormLiquid
Concentration0.5 mg/mL
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageStore at 4℃ short term (1-2 weeks). Store at -20℃ long term (24 months). Upon delivery aliquot. Avoid freeze/thaw cycle.

Images

TIMP2 Mouse mAb (Ab131343) - Western Blot
All lanes: TIMP2 Mouse mAb (Ab131343) at 1/2000 dilution
Samples: Lysates at 20 µg per lane
Secondary: Goat Anti-Mouse IgG H&L (HRP) (Ab138040) at 1/20000 dilution

Predicted band size: 24 kDa
Observed band size: 21 kDa
Exposure time: 120.0 s

TIMP2 Mouse mAb (Ab131343) - IF/ICC
Immunofluorescent analysis of 4% paraformaldehyde-fixed, 0.1% Triton X-100 permeabilized A549 (human lung adenocarcinoma epithelial cell line) cells labeling TIMP2 with TIMP2 Mouse mAb (Ab131343) at 1/25 dilution, followed by Dylight® 488-conjugated goat anti-mouse IgG secondary antibody at 1/200 dilution (green). Immunofluorescence image showing cytoplasm staining on A549 cell line. Cytoplasmic actin is detected with Dylight® 554 Phalloidin at 1/100 dilution (red). The nuclear counter stain is DAPI (blue).

TIMP2 Mouse mAb (Ab131343) - IHC
Immunohistochemical analysis of paraffin-embedded Human kidney section using TIMP2 Mouse mAb (Ab131343). TIMP2 Mouse mAb (Ab131343) was diluted at 1/200 dilution. A undiluted biotinylated goat polyvalent antibody was used as the secondary, followed by DAB staining.

TIMP2 Mouse mAb (Ab131343) - IHC
TIMP2 Mouse mAb (Ab131343) staining TIMP2 in human kidney sections by Immunohistochemistry. Tissue was fixed with formaldehyde and blocked with 3% BSA for 0.5 hour at room temperature; antigen retrieval was by heat mediation with a citrate buffer (pH 6.0). Samples were incubated with TIMP2 Mouse mAb (Ab131343) (1/25) for 1 hours at 37°C. A undiluted biotinylated goat polyvalent antibody was used as the secondary antibody.

TIMP2 Mouse mAb (Ab131343) - Flow Cytometry
Overlay histogram showing K562 cells stained with TIMP2 Mouse mAb (Ab131343) (green line). The cells were fixed with 2% paraformaldehyde (10 min) and then permeabilized with 90% methanol for 10 min. The cells were then icubated in 2% bovine serum albumin to block non-specific protein-protein interactions followed by the TIMP2 Mouse mAb (Ab131343) (1/25 dilution) for 60 min at 37ºC. The secondary antibody used was Goat-Anti-Mouse IgG, DyLight® 488 Conjugated Highly Cross-Adsorbed at 1/400 dilution for 40 min at 37ºC. Isotype control antibody (blue line) was mouse IgG1 (1μg/1x10^6 cells) used under the same conditions. Acquisition of >10000 events was performed.

Associated Targets(Human)

TIMP2 Tbio Metalloproteinase inhibitor 2 (0 Activities)
Activity TypeActivity Value -log(M)Mechanism of ActionActivity ReferencePublications (PubMed IDs)

Application

ApplicationDilution info
Flow Cytometry

1/25

WB1/2000

">

1/2000

IHC

1/200

IF/ICC

1/25

Certificates

Certificate of Analysis(COA)

Enter Lot Number to search for COA:

Find and download the COA for your product by matching the lot number on the packaging.

2 results found

Lot NumberChartCertificate TypeDateItem
ZJ24F0102591Certificate of AnalysisJan 25, 2024 Ab131343
ZJ24F0102590Certificate of AnalysisJan 25, 2024 Ab131343

Related Documents

References

1. Stetler-Stevenson, W G WG, Krutzsch, H C HC and Liotta, L A LA..  (1992)  TIMP-2: identification and characterization of a new member of the metalloproteinase inhibitor family..  Matrix (Stuttgart, Germany). Supplement,      [PMID:1480041]
2. Osthues, A A, Knäuper, V V, Oberhoff, R R, Reinke, H H and Tschesche, H H..  (1992)  Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid..  FEBS letters,    (13):   [PMID:1730286]
3. Boone, T C TC, Johnson, M J MJ, De Clerck, Y A YA and Langley, K E KE..  (1990)  cDNA cloning and expression of a metalloproteinase inhibitor related to tissue inhibitor of metalloproteinases..  Proceedings of the National Academy of Sciences of the United States of America,      [PMID:2157214]
4. Stetler-Stevenson, W G WG, Brown, P D PD, Onisto, M M, Levy, A T AT and Liotta, L A LA..  (1990)  Tissue inhibitor of metalloproteinases-2 (TIMP-2) mRNA expression in tumor cell lines and human tumor tissues..  The Journal of biological chemistry,    (15):   [PMID:2380196]
5. Goldberg, G I GI and 5 more authors..  (1989)  Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2..  Proceedings of the National Academy of Sciences of the United States of America,      [PMID:2554304]
6. Stetler-Stevenson, W G WG, Krutzsch, H C HC and Liotta, L A LA..  (1989)  Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family..  The Journal of biological chemistry,    (15):   [PMID:2793861]
7. Williamson, R A RA and 6 more authors..  (1994)  Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family..  Biochemistry,    (4):   [PMID:7918391]
8. De Clerck, Y A YA, Darville, M I MI, Eeckhout, Y Y and Rousseau, G G GG..  (1994)  Characterization of the promoter of the gene encoding human tissue inhibitor of metalloproteinases-2 (TIMP-2)..  Gene,    (25):   [PMID:8112602]
9. Hammani, K K and 6 more authors..  (1996)  Structure and characterization of the human tissue inhibitor of metalloproteinases-2 gene..  The Journal of biological chemistry,    (11):   [PMID:8810321]
10. Muskett, F W FW and 5 more authors..  (1998)  High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3..  The Journal of biological chemistry,    (21):   [PMID:9705310]
11. Tuuttila, A A and 8 more authors..  (1998)  Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 A resolution..  Journal of molecular biology,    (11):   [PMID:9837731]
12. Morgunova, Ekaterina E, Tuuttila, Ari A, Bergmann, Ulrich U and Tryggvason, Karl K..  (2002)  Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2..  Proceedings of the National Academy of Sciences of the United States of America,    (28):   [PMID:12032297]
13. Batra, Jyotica J, Soares, Alexei S AS, Mehner, Christine C and Radisky, Evette S ES..  (2013)  Matrix metalloproteinase-10/TIMP-2 structure and analyses define conserved core interactions and diverse exosite interactions in MMP/TIMP complexes..  PloS one,      [PMID:24073280]

Solution Calculators