TIMP Metallopeptidase Inhibitor 1 (TIMP1) (AA 24-207), (C-Term) (Active) Protein

Details zu Produkt Nr. ABIN2666716, 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 24-207, C-Term
17
5
5
2
2
1
1
1
1
1
1
1
1
1
1
Spezies
Human
30
8
6
2
2
2
2
1
1
1
1
Quelle
HEK-293
27
8
6
5
5
3
2
1
1
1
1
Protein-Typ
Recombinant
Biologische Aktivität
Active
Applikation
Western Blotting (WB)
Optionen
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Reinheit > 90 % , as determined by Coomassie stained SDS-PAGE.
Sterilität 0.22 μm filtered
Endotoxin-Niveau

Less than 1.0 EU per μg of protein as determine by the LAL method.

Hintergrund TIMPs (tissue inhibitors of metalloproteinases) are endogenous inhibitors for MMPs (matrix metalloproteinases). The human TIMPs consist of structurally and functionally distinct N- and C-terminal domains, each of which is stabilized by three disulfide bonds. The N-terminal domain binds to the active site of MMPs, inhibiting their proteolytic activities. The bidentate coordination of the zinc ion in the active site of an MMP by the N-terminal α-amino group and carbonyl group of the Cys residue in the "cysteine switch" motif is a key mechanism of inhibition with MMPs. The C-terminal domain is known to bind hemopexin-like domain of pro-MMPs. TIMPs are broad-spectrum inhibitors of MMPs, but there are some differences in specificity among them. Human metalloproteinase inhibitor 1, also named TIMP-1, is more restricted in its inhibitory range than the other three TIMPs, having a relatively low affinity for the membrane-type MMPs, MMP-14, MMP-16, and MMP-24 as well as for MMP-19. TIMP-1 is widely expressed in many mammalian tissues, notably in the reproductive organs. TIMP-1 is able to promote cell proliferation in a wide range of cell types and may also have an anti-apoptotic function. It has anti-angiogenic activity by preventing endothelial cell migration. CD63 has been identified as a receptor for TIMP-1. TIMP-1 binding to CD63 inhibits apoptosis and arrests cell growth. TIMP-1-null mice exhibit a number of alterations in processes associated with reproduction and steroidogenesis and impaired learning and memory.
Molekulargewicht Predicted molecular mass of approximately 22 kDa. The protein migrates at about 35 kDa in DTT-reducing conditions and about 30 kDa in non-reducing conditions by SDS-PAGE. The N-terminal amino acid is Cys.
Forschungsgebiet Extracellular Matrix, Cancer, Inflammation
Applikationshinweise Optimal working dilution should be determined by the investigator.
Kommentare

Biological activity: Human TIMP-1 inhibits the activity of activated mouse MMP-9 (100 ng/mL). The is IC50 ≤ 34 ng/mL.

Beschränkungen Nur für Forschungszwecke einsetzbar
Format Liquid
Rekonstitution For maximum results, quick spin vial prior to opening.
Buffer 0.22 μm filtered protein solution is in 10 mM sodium Acetate, 150 mM NaCl, pH 5.0.
Handhabung Avoid repeated freeze/thaw cycles.
Lagerung -20 °C
Informationen zur Lagerung Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for three months, or at -70°C for six months.
Allgemeine Veröffentlichungen Kim, Kim, Kang, Ko: "Expression level and glycan dynamics determine the net effects of TIMP-1 on cancer progression." in: BMB reports, Vol. 45, Issue 11, pp. 623-8, 2012 (PubMed).

Murphy: "Tissue inhibitors of metalloproteinases." in: Genome biology, Vol. 12, Issue 11, pp. 233, 2012 (PubMed).

Bourboulia, Stetler-Stevenson: "Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): Positive and negative regulators in tumor cell adhesion." in: Seminars in cancer biology, Vol. 20, Issue 3, pp. 161-8, 2010 (PubMed).

Brew, Nagase: "The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity." in: Biochimica et biophysica acta, Vol. 1803, Issue 1, pp. 55-71, 2010 (PubMed).