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>   首页   >   产品   >   一抗   >   癌症   >   Rabbit Anti-TIMP-2 Polyclonal Antibody   

Rabbit Anti-TIMP-2 Polyclonal Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - Rabbit Anti-TIMP-2 Polyclonal Antibody AP52136
    L1 and L2 rat lung lysates probed with Anti TIMP-2 Polyclonal Antibody, Unconjugated (AP52136) at 1:200 in 4˚C. Followed by conjugation to secondary antibody at 1:3000 90min in 37˚C. Predicted band 24kD. Observed band size: 21kD
  • 14 - Rabbit Anti-TIMP-2 Polyclonal Antibody AP52136
    Formalin-fixed and paraffin embedded rat kidney tissue labeled with Anti-TIMP-2 Polyclonal Antibody (AP52136), Unconjugated at 1:200, followed by conjugation to the secondary antibody and DAB staining
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, IHC-P, IHC-F, IF, E
Primary Accession P16035
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Calculated MW 24399 Da
Physical State Liquid
Immunogen KLH conjugated synthetic peptide derived from human TIMP-2
Epitope Specificity 131-220/220
Isotype IgG
Purity affinity purified by Protein A
Buffer 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
SUBCELLULAR LOCATION Secreted.
SIMILARITY Belongs to the protease inhibitor I35 (TIMP) family.Contains 1 NTR domain.
SUBUNIT Interacts (via the C-terminal) with MMP2 (via the C-terminal PEX domain); the interaction inhibits the MMP2 activity.
Post-translational modifications The activity of TIMP2 is dependent on the presence of disulfide bonds.
Important Note This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
Background Descriptions This gene is a member of the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. In addition to an inhibitory role against metalloproteinases, the encoded protein has a unique role among TIMP family members in its ability to directly suppress the proliferation of endothelial cells. As a result, the encoded protein may be critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors, and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix. [provided by RefSeq, Jul 2008].
Additional Information
Gene ID 7077
Other Names DDC8; CSC-21K; KIAA1731NL; Metalloproteinase inhibitor 2; Tissue inhibitor of metalloproteinases 2; TIMP-2; TIMP2
Dilution WB=1:500-2000,IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500,ELISA=1:5000-10000
Format0.01M TBS(pH7.4) with 1% BSA, 0.09% (W/V) sodium azide and 50% Glyce
StorageStore at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
Protein Information
Name TIMP2
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.
Cellular Location Secreted.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

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.

REFERENCES

Stetler-Stevenson W.G.,et al.J. Biol. Chem. 265:13933-13938(1990).
Boone T.C.,et al.Proc. Natl. Acad. Sci. U.S.A. 87:2800-2804(1990).
Hammani K.,et al.J. Biol. Chem. 271:25498-25505(1996).
Malik K.,et al.Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases.
Stetler-Stevenson W.G.,et al.J. Biol. Chem. 264:17374-17378(1989).

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