FITC Mouse Anti-Human TNF-α

BD FastImmune™ FITC Mouse Anti-Human TNF-α

Name: FITC Mouse Anti-Human TNF-α
Brand: FITC Mouse Anti-Human TNF-α
SKU: 340511

Clone 6401.1111 (RUO (GMP))

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Product Details

Brand: BD FastImmune™

Reactivity: Human

Isotype: Mouse IgG1

Immunogen: Recombinant human TNF-a

Application: Intracellular staining (flow cytometry)

Vol. Per Test: 20 μL

Entrez Gene ID: 7124

RRID: AB_400434

Storage Buffer: Phosphate buffered saline with gelatin and 0.1% sodium azide.

Regulatory Status: RUO (GMP)

Preparation And Storage

The FITC and PE conjugates are each supplied in 1.0 mL of PBS. The APC conjugate is supplied in 0.5 mL of PBS. Buffered saline contains gelatin and 0.1% sodium azide. Please refer to the vial label for antibody concentration. The vial should be stored at 2° to 8°C. Conjugated forms should not be frozen and should be protected from prolonged exposure to light. Each reagent is stable for the period shown on the bottle label when stored as directed.

340511 Rev. 1

Antibody Details

6401.1111

Anti-Hu–TNF-α, clone 6401.1111, is derived from a fusion of Sp2/0 myeloma cells with splenocytes from BALB/c mice immunized with recombinant human TNF-α.

Anti-Human Tumor Necrosis Factor-α (Anti-Hu–TNF-α) recognizes a 26-kilodalton (kd) transmembrane protein.

340511 Rev. 1

Format Details

FITC

Fluorescein (FITC) is part of the BD blue family of dyes. This is a small organic fluorochrome with an excitation maximum (Ex Max) at 494-nm and an emission maximum (Em Max) at 518-nm. FITC is designed to be excited by the Blue laser (488-nm) and detected using an optical filter centered near 520 nm (e.g., a 530/30-nm bandpass filter). Please ensure that your instrument’s configurations (lasers and optical filters) are appropriate for this dye.

Format: FITC

Excitation Max: 494 nm

Emission Max: 518 nm

340511 Rev.1

Citations & References

View product citations for antibody "340511" on CiteAb

Development References (19)

Aversa G, Punnonen J, de Vries JE. The 26-kD transmembrane form of tumor necrosis factor α on activated CD4+ T cell clones provides a co-stimulatory signal for human B cell activation. J Exp Med. 1993; 177:1575-1585. (Biology).
Beutler B, Cerami A. CachectMore than a tumor necrosis factor. N Eng J Med. 1987; 316:379-385. (Biology).
Beutler B, Cerami A. Tumor necrosis, cachexia, shock, and inﬂammation: a common mediator. Ann Rev Biochem. 1988; 57:505-518. (Biology).
Cassatella MA, Meda L, Bonora S, et al. Interleukin 10 (IL-10) inhibits the release of proinflammatory cytokines from human polymorphonuclear leukocytes. Evidence for an autocrine role of tumor necrosis factor and IL-1 β in mediating the production of IL-8 triggered by lipopolysaccharide. J Exp Med. 1993; 178:2207-2211. (Biology).
Decamps-Latscha B, Herbelin A, Nguyen AT, et al. Balance between IL-1β, TNF-α, and their specific inhibitors in chronic renal failure and maintenance dialysis. Relationships with activation markers of T cells, B cells, and monocytes. J Immunol. 1995; 154:882-892. (Biology).
Hsu H, Shu HB, Pan MG, Goeddel DV. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell. 1996; 84(2):299-308. (Biology). View Reference
Jones EY, Stuart DI, Walker NPC. Structure of tumour necrosis factor. Nature. 1989; 338:225-228. (Biology).
Kinkhabwala M Sehajpal P, Skolnik E, et al. A novel addition to the T cell repertory, Cell surface expression of tumor necrosis factor/cachectin by activated normal human T cells. J Exp Med. 1990; 171:941-946. (Biology).
Kriegler M, Perez C, DeFay K, Albert I, Lu SD. A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF. Cell. 1988; 53(1):45-53. (Biology). View Reference
Martich GD, Danner RL, Ceska M, et al. Detection of interleukin 8 and tumor necrosis factor in normal humans after intravenous endotoxThe effect of anti-inflammatory agents. J Exp Med. 1991; 173:1021-1024. (Biology).
Mestan J, Digel W, Mittnacht S, et al. Antiviral effects of tumour necrosis factor in vitro. Nature. 1986; 323:816-819. (Biology).
Michie HR, Manogue KR, Spriggs DR, et al. Detection of circulating tumor necrosis factor after endotoxin administration. N Eng J Med. 1988; 318:1481-1486. (Biology).
Old LJ. Tumor necrosis factor (TNF). Science. 1985; 230:630-632. (Biology).
Saklatvala J. Tumour necrosis factor α stimulates resorption and inhibits synthesis of proteoglycan in cartilage. Science. 1986; 322:547-549. (Biology).
Smith CA, Farrah T, Goodwin RG. The TNF receptor superfamily of cellular and viral proteins: activation, costimulation, and death. Cell. 1994; 76(6):959-962. (Biology). View Reference
Sung SJ, Bjorndahl JM, Wang CY, et al. Production of tumor necrosis factor/cachectin by human B cell lines and tonsillar B cells. J Exp Med. 1988; 168:1539-1551. (Biology).
Sypek JP, Wyler DJ. Antileishmanial defense in macrophages triggered by tumor necrosis factor expressed on CD4+ T lymphocyte plasma membrane. J Exp Med. 1991; 174:755-759. (Biology).
Tracey KJ, Beutler B, Lowry SF, et al. Shock and tissue injury induced by recombinant human cachectin. Science. 1986; 234:470-474. (Biology).
Wong GH, Goeddel D. Tumour necrosis factors α and β inhibit virus replication and synergize with interferons. Nature. 1986; 323:819-822. (Biology).

View All (19)

340511 Rev. 1

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