ArtNr |
IT3-H52W8-1mg |
Hersteller |
ACROBiosystems
|
Menge |
1 mg |
Kategorie |
|
Typ |
Proteins Recombinant |
Format |
Powder |
Specific against |
Human |
Host |
HEK293 |
Konjugat/Tag |
Unconjugated, HIS |
Purity |
90% |
Citations |
(1) Leisner TM., et al., 1999, J. Biol. Chem. 274:12945-12949. (2) Basani RB., et al., 1996, Blood. 88:167-173. |
ECLASS 10.1 |
32160409 |
ECLASS 11.0 |
32160409 |
UNSPSC |
12352202 |
Alias |
Integrin alpha 2b beta 3,ITGAIIb&ITGB3 |
Lieferbar |
|
Manufacturers Category |
Protein / Bio-Markers & CD Antigens |
Description |
Human ITGAIIb&ITGB3 Heterodimer Protein, His Tag&Tag Free (IT3-H52W8) is expressed from human 293 cells (HEK293). It contains AA Leu 32 - Arg 993 (ITGAIIb) & Gly 27 - Asp 718 (ITGB3) (Accession # P08514-1 (ITGAIIb) & P05106-1 (ITGB3)). |
Molecule |
Integrin alpha 2b beta 3 |
Exp Region |
Leu 32 - Arg 993 (ITGAIIb) & Gly 27 - Asp 718 (ITGB3) |
Storage |
-20℃ |
Shipping |
RT |
Stability |
-20°C to -70°C for 12 months in lyophilized state; -70°C for 3 months under sterile conditions after reconstitution.
For long term storage, the product should be stored at lyophilized state at -20°C or lower. |
Molecular Weight |
111.4 kDa (ITGAIIb) & 81.8 kDa (ITGB3) |
Characteristics |
Human ITGAIIb&ITGB3 Heterodimer Protein, His Tag&Tag Free, produced by co-expression of ITGAIIb and ITGB3, has a calculated MW of 111.4 kDa (ITGAIIb) and 81.8 kDa (ITGB3). Subunit ITGAIIb is fused with an acidic tail at the C-terminus and followed by a polyhistidine tag and subunit ITGB3 contains no tag but a basic tail at the C-terminus. The non-reducing (NR) protein migrates as 115-130 kDa (ITGAIIb) and 85-92 kDa (ITGB3) respectively due to glycosylation. |
Endotoxin |
1.0 EU per μg |
Buffer |
50 mM Tris, 150 mM NaCl, pH7.5 |
Background |
Integrin alpha IIb beta 3 exist in a conformational equilibrium clustered around four main states. These conformations range from a compact bent nodule to two partially extended intermediate conformers and finally to a fully upright state. Activation of blood platelets by physiological stimuli at sites of vascular injury induces inside-out signaling, resulting in a conformational change of the prototype Integrin alpha IIb beta 3 from an inactive to an active state competent to bind soluble fibrinogen. Furthermore, ligand occupancy of Integrin alpha IIb beta 3 outside-in signaling and additional conformational changes of the receptor, leading to the exposure of extracellular neoepitopes termed ligand-induced binding sites (LIBS), which are recognized by anti-LIBS monoclonal antibodies. |
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