Retinol Binding Protein 4, Plasma (RBP4) (AA 1-201), (Extracellular Domain) (Active) protein (His tag)

Details zu Produkt Nr. ABIN2009021, Anbieter: Anmelden zum Anzeigen
Proteinname
  • rbp4
  • MGC54038
  • srbp
  • 2310002G05Rik
  • 2610028L19Rik
  • HSRBP4
  • RBP4
  • RBP
  • RNBP
  • RDCCAS
  • Rbp-4
  • RBPA
  • PRBP
  • retinol binding protein 4, plasma
  • polymerase (RNA) II (DNA directed) polypeptide D
  • renin binding protein
  • rbp4
  • Polr2d
  • RENBP
  • RBP4
  • Rbp4
Proteineigenschaft
AA 1-201, Extracellular Domain
25
8
5
2
1
1
1
1
1
1
1
1
1
1
1
1
1
Spezies
Ratte (Rattus)
39
11
8
4
3
2
2
2
1
1
1
1
1
Quelle
Human Cells
25
12
10
6
6
5
2
2
1
Protein-Typ
Recombinant
Biologische Aktivität
Active
Aufreinigungstag / Konjugat
Dieses RBP4 Protein ist gelabelt mit His tag.
Applikation
Functional Studies (Func), SDS-PAGE (SDS)
Optionen
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Produktmerkmale The recombinant rat RBP4 comprises 194 amino acids and predicts a molecular mass of 22.8 kDa. The apparent molecular mass of the rat RBP4 is approximately 24 kDa in SDS-PAGE under reducing conditions.

Protein Structure: A DNA sequence encoding the extracellular domain of rat RBP4 (NP_037294.1) (Met 1-Leu 201) was expressed, fused with a polyhistidine tag at the C-terminus.
Predicted N-Term: Glu 19
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 bind alltrans retinoic acid. The binding of retinoic acid results in the quenching of Trp fluorescence in RBP4.
The 50% binding concentration (BC50) is >0.5 μM
Molekulargewicht 22.8 kDa, 24 kDa
NCBI Accession NP_037294
Forschungsgebiet Cardiovascular, Atherosclerosis, Metabolism, Hormones, Cytokines
Pathways Regulatorische RNA Pathways, Positive Regulation of Peptide Hormone Secretion, Carbohydrate Homeostasis, Production of Molecular Mediator of Immune Response
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 Retinol Binding Protein 4, Plasma (RBP4) (AA 1-201), (Extracellular Domain) (Active) protein (His tag) (ABIN2009021) Retinol Binding Protein 4, Plasma (RBP4) (AA 1-201), (Extracellular Domain) (Active) protein (His tag)
Allgemeine Veröffentlichungen Balagopal, Graham, Kahn, Altomare, Funanage, George: "Reduction of elevated serum retinol binding protein in obese children by lifestyle intervention: association with subclinical inflammation." in: The Journal of clinical endocrinology and metabolism, Vol. 92, Issue 5, pp. 1971-4, 2007 (PubMed).

Cho, Youn, Lee, Lee, Min, Kwak, Lee, Park: "Plasma retinol-binding protein-4 concentrations are elevated in human subjects with impaired glucose tolerance and type 2 diabetes." in: Diabetes Care, Vol. 29, Issue 11, pp. 2457-61, 2006 (PubMed).

Zanotti, Berni: "Plasma retinol-binding protein: structure and interactions with retinol, retinoids, and transthyretin." in: Vitamins and hormones, Vol. 69, pp. 271-95, 2004 (PubMed).

Quadro, Blaner, Hamberger, Van Gelder, Vogel, Piantedosi, Gouras, Colantuoni, Gottesman: "Muscle expression of human retinol-binding protein (RBP). Suppression of the visual defect of RBP knockout mice." in: The Journal of biological chemistry, Vol. 277, Issue 33, pp. 30191-7, 2002 (PubMed).

Colantuoni, Romano, Bensi, Santoro, Costanzo, Raugei, Cortese: "Cloning and sequencing of a full length cDNA coding for human retinol-binding protein." in: Nucleic acids research, Vol. 11, Issue 22, pp. 7769-76, 1984 (PubMed).