Thermo Fisher Scientific SARS-CoV-2 surface glycoprotein Polyclonal Antibody, FITC
SARS-CoV-2 스파이크 단백질을 인식하는 FITC 결합 폴리클로날 항체. Western blot, ELISA, IP에 사용 가능. 토끼 유래 IgG 형태로 형광 검출에 적합. 연구용으로만 사용.
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Applications and Tested Dilution
| Application | Tested Dilution |
|---|---|
| Western Blot (WB) | 1:500–1:1,000 |
| ELISA | 1:10,000 |
| Immunoprecipitation (IP) | 1:50–1:250 |
Product Specifications
| 항목 | 내용 |
|---|---|
| Species Reactivity | Virus |
| Host / Isotype | Rabbit / IgG |
| Class | Polyclonal |
| Type | Antibody |
| Immunogen | Synthetic peptide taken from unique amino acid sequence on surface glycoprotein (Severe acute respiratory syndrome coronavirus 2) |
| Conjugate | FITC (Fluorescein isothiocyanate) |
| Excitation / Emission Max | 498 / 517 nm |
| Form | Liquid |
| Concentration | 0.5–1.5 mg/mL |
| Purification | Affinity chromatography |
| Storage Buffer | Proprietary buffer, pH 7.4–7.8, with 30% glycerol, 0.5% BSA |
| Contains | 0.02% sodium azide |
| Storage Conditions | −20°C, store in dark |
| Shipping Conditions | Ambient (domestic); Wet ice (international) |
Target Information
SARS-CoV-2 (Severe Acute Respiratory Syndrome Coronavirus 2), also known as 2019-nCoV, is a virus that causes illnesses ranging from mild cold-like symptoms to severe respiratory distress and death.
The CoV Spike (S) protein plays a crucial role in viral attachment, fusion, and entry, making it a key target for antibody development, entry inhibitors, and vaccines.
The Spike protein receptor-binding domain (RBD, S-RBD) binds strongly to human and bat ACE2 receptors, exhibiting higher affinity compared to SARS-CoV RBD.
S1 contains the RBD responsible for ACE2 binding, while S2 mediates membrane fusion. The SARS-CoV-2 S protein consists of 1273 amino acids, including a signal peptide (1–13), S1 subunit (14–685), and S2 subunit (686–1273). The extracellular domain (S-ECD) corresponds to the Spike protein’s external region.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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