CD134 IgG2a Fc, Fusion Protein (OX40) (Biotin)

Cat# C2515-26B-25ug

Size : 25ug

Brand : US Biological

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C2515-26B CD134 IgG2a Fc, Fusion Protein (OX40) (Biotin)

Clone Type
Polyclonal
Grade
Affinity Purified
Applications
E FC
Shipping Temp
Blue Ice
Storage Temp
4°C

Human CD134 (OX40) (ACT35) is an activation-associated antigen which is predominantly expressed on activated CD4 positive cells. CD134 antigen is a member of the tumor necrosis factor (TNF) receptor family of molecules and may be involved with regulating T cell-dependent B cell proliferation and differentiation (2).||Molecular Structure: A soluble fusion protein consisting of the extracellular (185 aa) domain of  human CD134 fused to murine IgG2a Fc (232 aa), with a predicted monomeric molecular weight of 45.6 kd.||Transfectant Cell Line: CHO||Functional Application: CD134-muIg fusion protein blocks binding of anti-human CD134 to human tumor cells.||Applications: |Suitable for use in ELISA, Flow cytometry. Other applications not tested.||stor4

Applications
Source: CHO cells|Purity: Purified by affinity chromatography prior to conjugation.|Concentration: ~0.5mg/ml|Form: Supplied as a liquid in 50mM sodium phosphate pH 7.5, 100mM potassium chloride,, 150mM sodium chloride, 0.2% BSA, 0.04% sodium azide, 5% glycerol. Labeled with Biotin.||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Form
Supplied as a liquid in 50mM sodium phosphate pH 7.5, 100mM potassium chloride, 150mM sodium chloride, 0.2% BSA, 0.04% sodium azide, 5% glycerol. Labeled with Biotin.|
Purity
Purified by affinity chromatography prior to conjugation.
References
1. U. Latza, et al, (1994) Eur J Immunol 24: 677-683. 2. E. Stuber, et al, (1995) Immunity 2: 507-521. 3. Leukocyte Typing IV (W. Knapp, et al, eds.) Oxford University Press, Oxford, (1989) p. 464-465. 4. Leukocyte Typing V (S.F. Schlossman, et al, eds.) Oxford University Press, Oxford, (1995) p. 1157-1160.