TIMP1 Antibody - Primary antibody, specific to TIMP1, Rabbit IgG

    Application:
  • WB
Features and benefits
  • Host species: Rabbit
  • Species reactivity(Reacts with): Human
  • Isotype: Rabbit IgG
  • Conjugation: Unconjugated
Item Number
Ab131327
Grouped product items
SKUSizeAvailabilityPrice Qty
Ab131327-10μl
10μl
In stock
$66.90
Ab131327-50μl
50μl
In stock
$189.90
Ab131327-100μl
100μl
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$299.90
Ab131327-1ml
1ml
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$2,809.90

pAb; Rabbit anti Human TIMP1 Antibody; WB; Unconjugated

Basic Description

Product NameTIMP1 Antibody - Primary antibody, specific to TIMP1, Rabbit IgG
SynonymsClgi antibody | Collagenase inhibitor antibody | Collagenase inhibitor, Human antibody | EPA antibody | EPO antibody | Erythroid Potentiating Activity antibody | Erythroid-potentiating activity antibody | Fibroblast collagenase inhibitor antibody | FLJ903
Specifications & PurityExactAb™, Validated, 2.6 mg/mL
Host speciesRabbit
SpecificityTIMP1
ImmunogenA synthetic peptide derived from human TIMP1 (AA 1-207).
Positive ControlWB: HT-29, SK-OV-3 and HeLa cell lysates.
ConjugationUnconjugated
GradeExactAb™, Validated
Product Description

Rabbit anti Human TIMP1 Antibody, Polyclonal antibody, could be used for WB and so on.
Application:
WB: 1/500-1/1000
Protein Function:
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. Does not act on MMP-14.

Product Properties

IsotypeRabbit IgG
SDS-PAGE150 kDa
Purification MethodProtein A purified
FormLiquid
Concentration2.6 mg/mL
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageStore at 4°C short term (1-2 weeks). Store at -20°C long term (24 months). Upon delivery aliquot. Avoid freeze/thaw cycle.

Images

TIMP1 Antibody (Ab131327) - Western Blot
All lanes: TIMP1 Antibody (Ab131327) at 1/1000 dilution
Samples: Lysates at 20 µg per lane
Secondary: Goat Anti-Rabbit IgG H&L (HRP) (Ab170144) at 1/20000 dilution

Predicted band size: 23 kDa
Observed band size: 28 kDa
Exposure time: 1.0 s

Associated Targets(Human)

TIMP1 Tbio Metalloproteinase inhibitor 1 (0 Activities)
Activity TypeActivity Value -log(M)Mechanism of ActionActivity ReferencePublications (PubMed IDs)

Application

ApplicationDilution info
WB1/500-1/1000

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1/500-1/1000

Certificates

Certificate of Analysis(COA)

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2 results found

Lot NumberChartCertificate TypeDateItem
ZJ24F0403964Certificate of AnalysisApr 01, 2024 Ab131327
ZJ24F0403965Certificate of AnalysisApr 01, 2024 Ab131327

Related Documents

References

1. O'Shea, M M and 7 more authors..  (1992)  Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13..  Biochemistry,    (27):   [PMID:1420137]
2. Van Ranst, M M and 7 more authors..  (1991)  The cytokine-protease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers..  Cytokine,      [PMID:1653055]
3. 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]
4. Williamson, R A RA and 9 more authors..  (1990)  Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)..  The Biochemical journal,    (1):   [PMID:2163605]
5. Rapp, G G and 6 more authors..  (1990)  Characterization of three abundant mRNAs from human ovarian granulosa cells..  DNA and cell biology,      [PMID:2171551]
6. Carmichael, D F DF and 6 more authors..  (1986)  Primary structure and cDNA cloning of human fibroblast collagenase inhibitor..  Proceedings of the National Academy of Sciences of the United States of America,      [PMID:3010309]
7. Docherty, A J AJ and 7 more authors..  (1985)  Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity..  Nature,      [PMID:3903517]
8. Opbroek, A A, Kenney, M C MC and Brown, D D..  (1993)  Characterization of a human corneal metalloproteinase inhibitor (TIMP-1)..  Current eye research,      [PMID:7507419]
9. Knäuper, V V, López-Otin, C C, Smith, B B, Knight, G G and Murphy, G G..  (1996)  Biochemical characterization of human collagenase-3..  The Journal of biological chemistry,    (19):   [PMID:8576151]
10. Knäuper, V V and 7 more authors..  (1997)  The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction..  The Journal of biological chemistry,    (21):   [PMID:9065415]
11. Hardcastle, A J AJ, Thiselton, D L DL, Nayudu, M M, Hampson, R M RM and Bhattacharya, S S SS..  (1997)  Genomic organization of the human TIMP-1 gene. Investigation of a causative role in the pathogenesis of X-linked retinitis pigmentosa 2..  Investigative ophthalmology & visual science,      [PMID:9286280]
12. Gomis-Rüth, F X FX and 11 more authors..  (1997)  Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1..  Nature,    (4):   [PMID:9288970]
13. Wu, B B and 7 more authors..  (2000)  NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases..  Journal of molecular biology,    (14):   [PMID:10623524]
14. Zhang, Zemin Z and Henzel, William J WJ..  (2004)  Signal peptide prediction based on analysis of experimentally verified cleavage sites..  Protein science : a publication of the Protein Society,      [PMID:15340161]
15. Lewandrowski, Urs U, Moebius, Jan J, Walter, Ulrich U and Sickmann, Albert A..  (2006)  Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach..  Molecular & cellular proteomics : MCP,      [PMID:16263699]
16. Liu, Tao T and 6 more authors..  ()  Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry..  Journal of proteome research,      [PMID:16335952]
17. Ramachandran, Prasanna P and 5 more authors..  (2006)  Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry..  Journal of proteome research,      [PMID:16740002]
18. Jung, Ki-Kyung KK, Liu, Xu-Wen XW, Chirco, Rosemarie R, Fridman, Rafael R and Kim, Hyeong-Reh Choi HR..  (2006)  Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein..  The EMBO journal,    (6):   [PMID:16917503]
19. Iyer, Shalini S, Wei, Shuo S, Brew, Keith K and Acharya, K Ravi KR..  (2007)  Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1..  The Journal of biological chemistry,    (5):   [PMID:17050530]
20. Grossman, Moran M and 6 more authors..  (2010)  The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function..  Biochemistry,    (27):   [PMID:20545310]
21. Batra, Jyotica J and 5 more authors..  (2012)  Matrix metalloproteinase-10 (MMP-10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure..  The Journal of biological chemistry,    (4):   [PMID:22427646]
22. Rosenow, Anja A and 6 more authors..  (2012)  Resveratrol-induced changes of the human adipocyte secretion profile..  Journal of proteome research,    (7):   [PMID:22905912]
23. Toricelli, Mariana M, Melo, Fabiana H M FH, Peres, Giovani B GB, Silva, Débora C P DC and Jasiulionis, Miriam G MG..  (2013)  Timp1 interacts with beta-1 integrin and CD63 along melanoma genesis and confers anoikis resistance by activating PI3-K signaling pathway independently of Akt phosphorylation..  Molecular cancer,    (25):   [PMID:23522389]
24. Lee, Soo Youn SY and 9 more authors..  (2014)  TIMP-1 modulates chemotaxis of human neural stem cells through CD63 and integrin signalling..  The Biochemical journal,    (1):   [PMID:24635319]
25. Tagliabracci, Vincent S VS and 14 more authors..  (2015)  A Single Kinase Generates the Majority of the Secreted Phosphoproteome..  Cell,    (18):   [PMID:26091039]
26. Gasson, J C JC and 9 more authors..  (1985)  Molecular characterization and expression of the gene encoding human erythroid-potentiating activity..  Nature,      [PMID:3839290]

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