TIMP Metallopeptidase Inhibitor 1 (TIMP1) (AA 1-207) (Active) protein (His tag)

Details zu Produkt Nr. ABIN2003616, Anbieter: Anmelden zum Anzeigen
Proteinname
  • TIMP-1
  • TIMP1
  • DKFZp468A0912
  • CLGI
  • EPA
  • EPO
  • HCI
  • TIMP
  • Timp
  • Clgi
  • TIMP metallopeptidase inhibitor 1
  • tissue inhibitor of metalloproteinase 1
  • TIMP1
  • Timp1
  • LOC100009047
Proteineigenschaft
AA 1-207
20
3
3
2
2
1
1
1
1
1
1
1
1
1
1
Spezies
Human
33
6
3
2
2
2
2
1
1
1
1
Quelle
Human Cells
22
8
6
5
5
4
4
1
1
1
1
Protein-Typ
Recombinant
Biologische Aktivität
Active
Aufreinigungstag / Konjugat
Dieses TIMP1 Protein ist gelabelt mit His tag.
Applikation
Functional Studies (Func), SDS-PAGE (SDS)
Optionen
Hersteller
Anmelden zum Anzeigen
Hersteller Produkt- Nr.
Anmelden zum Anzeigen
Produktmerkmale The secreted recombinant human TIMP1 comprises 195 amino acids with a predicted molecular mass of 22 kDa. As a result of glycosylation, rhTIMP1 migrates as an approximately 30 kDa band in SDS-PAGE under reducing conditions.

Protein Structure: A DNA sequence encoding the human TIMP1 (NP_003245.1) (Met 1-Ala 207) with a C-terminal polyhistidine tag was expressed.
Predicted N-Term: Cys 24
Reinheit > 97 % as determined by SDS-PAGE
Endotoxin-Niveau < 1.0 EU per μg of the protein as determined by the LAL method
ProductDetails: Biological Activity Comment Measured by its ability to inhibit human MMP-2 cleavage of a fluorogenic peptide substrate MCA-PLGL-DPA-AR-NH2 . The IC50 value is < 6 nM.
Hintergrund Synonyms: CLGI,EPA,EPO,HCI,TIMP,TIMP-1
Molekulargewicht 22 kDa, 30 kDa
NCBI Accession NP_003245
Forschungsgebiet Proteolysis / Ubiquitin, Angiogenesis, Extracellular Matrix, Matrix Metalloproteinases, Cancer, Inflammation
Applikationshinweise Optimal working dilution should be determined by the investigator.
Beschränkungen Nur für Forschungszwecke einsetzbar
Format Lyophilized
Buffer Lyophilized from sterile PBS, pH 7.4
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization.
Handhabung Avoid repeated freeze-thaw cycles. It is recommended that the protein be aliquoted for optimal storage.
Lagerung -20 °C,-80 °C
Informationen zur Lagerung Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Shipping: In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Haltbarkeit 12 months
Bilder des Herstellers
 image for TIMP Metallopeptidase Inhibitor 1 (TIMP1) (AA 1-207) (Active) protein (His tag) (ABIN2003616) TIMP Metallopeptidase Inhibitor 1 (TIMP1) (AA 1-207) (Active) protein (His tag)
Allgemeine Veröffentlichungen Aljada, Ramnath, Donohue, Harvey, Brooks, Wiseman, Khoury, Loewen, Slocum, Anderson, Bepler, Tan: "Upregulation of the tissue inhibitor of metalloproteinase-1 protein is associated with progression of human non-small-cell lung cancer." in: Journal of clinical oncology : official journal of the American Society of Clinical Oncology, Vol. 22, Issue 16, pp. 3218-29, 2004

Aljada, Ramnath, Donohue, Harvey, Brooks, Wiseman, Khoury, Loewen, Slocum, Anderson, Bepler, Tan: "Upregulation of the tissue inhibitor of metalloproteinase-1 protein is associated with progression of human non-small-cell lung cancer." in: Journal of clinical oncology : official journal of the American Society of Clinical Oncology, Vol. 22, Issue 16, pp. 3218-29, 2004 (PubMed).

Hornebeck: "Down-regulation of tissue inhibitor of matrix metalloprotease-1 (TIMP-1) in aged human skin contributes to matrix degradation and impaired cell growth and survival." in: Pathologie-biologie, Vol. 51, Issue 10, pp. 569-73, 2003 (PubMed).

Gardner, Ghorpade: "Tissue inhibitor of metalloproteinase (TIMP)-1: the TIMPed balance of matrix metalloproteinases in the central nervous system." in: Journal of neuroscience research, Vol. 74, Issue 6, pp. 801-6, 2003 (PubMed).

Osthues, Knäuper, Oberhoff, Reinke, Tschesche: "Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid." in: FEBS letters, Vol. 296, Issue 1, pp. 16-20, 1992 (PubMed).

Haben Sie etwas anderes gesucht?