Recombinant Human IFNAR2 protein (Fc Chimera) (ab83680)
Key features and details
- Expression system: HEK 293 cells
- Purity: > 95% SDS-PAGE
- Tags: Fc tag C-Terminus
- Suitable for: Functional Studies, SDS-PAGE
製品の詳細
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製品名
Recombinant Human IFNAR2 protein (Fc Chimera)
IFNAR2 タンパク質・ペプチド 製品一覧 -
生理活性
ab83680 bound to protein A sepharose beads was able to pull down its ligand, IFNa2b. -
精製度
> 95 % SDS-PAGE. -
発現系
HEK 293 cells -
アクセッション番号
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タンパク質長
Full length protein -
Animal free
No -
由来
Recombinant -
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生物種
Human -
配列
Theoretical Sequence ISYDSPDYTDESCTFKISLRNFRSILSWELKNHSIVPTHYTLLYTIMSKP EDLKVVKNCANTTRSFCDLTDEWRSTHEAYVTVLEGFSGNTTLFSCSHNF WLAIDMSFEPPEFEIVGFTNHINVMVKFPSIVEEELQFDLSLVIEEQSEG IVKKHKPEIKGNMSGNFTYIIDKLIPNTNYCVSVYLEHSDEQAVIKSPLK CTLLPPGQESESAESAKGSSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNA KTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTIS KAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQP ENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYT QKSLSLSPGK -
領域
1 to 243 -
タグ
Fc tag C-Terminus -
配列の追加情報
Fused with the Fc region of Human IgG1 at the C-terminus.
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関連製品
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Related Products
特性
Our Abpromise guarantee covers the use of ab83680 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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アプリケーション
Functional Studies
SDS-PAGE
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製品の状態
Lyophilized -
備考
ab83680 bound to protein A sepharose beads was able to pull down its ligand, IFNa2b. -
Concentration information loading...
前処理および保存
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保存方法および安定性
Shipped at 4°C. After reconstitution store at -20ºC. Avoid freeze / thaw cycles.
Constituents: PBS, 1% Human serum albumin, 10% Trehalose
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再構成It is recommended that 0.5 ml of sterile phosphate-buffered saline be added to the vial. Following reconstitution short-term storage at 4°C is recommended, and longer-term storage of aliquots at -18 to -20°C. Repeated freeze thawing is not recommended.
関連情報
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別名
- Human interferon alpha/beta receptor
- IFN alpha REC
- IFN R
see all -
機能
Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 3 is a potent inhibitor of type I IFN receptor activity. -
組織特異性
Isoform 3 is detected in the urine (at protein level). Expressed in blood cells. Expressed in lymphoblastoid and fibrosarcoma cell lines. -
配列類似性
Belongs to the type II cytokine receptor family. -
翻訳後修飾
Phosphorylated on tyrosine residues upon interferon binding. Phosphorylation at Tyr-337 or Tyr-512 are sufficient to mediate interferon dependent activation of STAT1, STAT2 and STAT3 leading to antiproliferative effects on many different cell types.
Glycosylated. -
細胞内局在
Secreted and Membrane. - Information by UniProt
画像
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Densitometry of protein isoforms visualised by 2-DE. The triangle indicates the theoretical MW and pI of the protein.
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1D SDS-PAGE of ab83680 before and after treatment with glycosidases to remove oligosaccharides.
Lane 1 MW markers; Lane 2 ab83680; Lane 3 ab83680 treated with PNGase F to remove potential N-linked glycans; Lane 4 ab83680 treated with a glycosidase cocktail to remove potential N- and O-linked glycans. Approximately 5 μg of protein was loaded per lane.Drop in MW after treatment with PNGase F indicates presence of N-linked glycans. A further drop in MW after treatment with the glycosidase cocktail indicates the presence of O-linked glycans. Additional bands in lane 3 and lane 4 are glycosidase enzymes.
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A sample of ab83680 without carrier protein was reduced and alkylated and focused on a 3-10 IPG strip then run on a 4-20% Tris-HCl 2D gel. Approximately 40 μg of protein was load; Gel was stained using Deep Purple™.
プロトコール
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
データシートおよび資料
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SDS download
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Datasheet download
参考文献 (0)
ab83680 は論文での使用が確認できていません。