Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 (SERPINC1) (AA 1-464) (Active) protein (His tag)

Details zu Produkt Nr. ABIN2002163, Anbieter: Anmelden zum Anzeigen
Proteinname
  • AT3
  • AT3D
  • ATIII
  • THPH7
  • SERPINC1
  • DKFZp470C1733
  • AI114908
  • At-3
  • At3
  • ANTITHROMBIN, AT-III
  • AT-III
  • serpin peptidase inhibitor, clade C (antithrombin), member 1
  • antithrombin-III
  • serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1
  • SERPINC1
  • CpipJ_CPIJ000472
  • CpipJ_CPIJ013111
  • Serpinc1
Proteineigenschaft
AA 1-464
5
2
2
1
1
1
1
Spezies
Human
19
4
4
2
1
1
1
1
Quelle
Human Cells
11
9
2
2
2
1
1
1
1
1
1
Protein-Typ
Recombinant
Biologische Aktivität
Active
Aufreinigungstag / Konjugat
His tag
Applikation
Functional Studies (Func), SDS-PAGE (SDS)
Optionen
Hersteller
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Hersteller Produkt- Nr.
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Produktmerkmale The recombinant human SerpinC1 consists of 443 amino acids and has a predicted molecular mass of 50.5 kDa. In SDS-PAGE, the apparent molecular mass of rhSerpinC1 is approximately 55-60 kDa due to glycosylation.

Protein Structure: A DNA sequence encoding the human SerpinC1 (NP_000479.1) (Met 1-Lys 464) was expressed with a C-terminal polyhistidine tag.
Predicted N-Term: His 33
Reinheit > 95 % 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 thrombin (Sigma, Catalog # T4648)cleavage of a fluorogenic peptide substrate Boc-VPR-AMC.
The IC50 value is < 5 nM.
Hintergrund Synonyms: AT3,AT3D,ATIII,MGC22579,SerpinC1,THPH7
Molekulargewicht 50.5 kDa, 55-60 kDa
NCBI Accession NP_000479
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 Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 (SERPINC1) (AA 1-464) (Active) protein (His tag) (ABIN2002163) Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 (SERPINC1) (AA 1-464) (Active) protein (His tag)
Allgemeine Veröffentlichungen Saito, Minamiya, Kalina, Saito, Ogawa: "Effect of antithrombin III on neutrophil deformability." in: Journal of leukocyte biology, Vol. 78, Issue 3, pp. 777-84, 2005

Saito, Minamiya, Kalina, Saito, Ogawa: "Effect of antithrombin III on neutrophil deformability." in: Journal of leukocyte biology, Vol. 78, Issue 3, pp. 777-84, 2005 (PubMed).

Oelschläger, Römisch, Staubitz, Stauss, Leithäuser, Tillmanns, Hölschermann: "Antithrombin III inhibits nuclear factor kappaB activation in human monocytes and vascular endothelial cells." in: Blood, Vol. 99, Issue 11, pp. 4015-20, 2002 (PubMed).

Chuang, Swanson, Raja, Bock, Olson et al.: "The antithrombin P1 residue is important for target proteinase specificity but not for heparin activation of the serpin. Characterization of P1 antithrombin variants with altered proteinase ..." in: Biochemistry, Vol. 40, Issue 22, pp. 6670-9, 2001 (PubMed).

Perry: "Antithrombin and its inherited deficiencies." in: Blood reviews, Vol. 8, Issue 1, pp. 37-55, 1994 (PubMed).

Chandra, Stackhouse, Kidd, Woo: "Isolation and sequence characterization of a cDNA clone of human antithrombin III." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 80, Issue 7, pp. 1845-8, 1983 (PubMed).

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