01-675-622
SARS Coronavirus Nucleocapsid Polyclonal Antibody, Invitrogen™
Manufacturer: Thermo Scientific
Select a Size
| Pack Size | SKU | Availability | Price |
|---|---|---|---|
| Each of 1 | 01-675-622-Each-of-1 | In Stock | ₹ 46,057.50 |
01-675-622 - Each of 1
In Stock
Quantity
1
Base Price: ₹ 46,057.50
GST (18%): ₹ 8,290.35
Total Price: ₹ 54,347.85
Antigen
SARS Coronavirus Nucleocapsid
Classification
Polyclonal
Conjugate
Unconjugated
Gene Alias
Coronavirus; COVID; COVID 19; COVID19; COVID-19; SARS; SARS Coronavirus; SARS CoV; SARS CoV2; SARS CoV-2; SARS Nucleocapsid; SARS-CoV2; SARS-CoV-2
Immunogen
Synthetic peptide corresponding to residues 354-370 of putative SARS nucleocapsid.
Quantity
100 μg
Primary or Secondary
Primary
Content And Storage
Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.
Form
Liquid
Applications
ELISA, Immunocytochemistry, Immunohistochemistry (Paraffin), Western Blot
Concentration
1 mg/mL
Formulation
PBS with 0.05% sodium azide
Host Species
Rabbit
Purification Method
Protein G
Regulatory Status
RUO
Target Species
Virus
Product Type
Antibody
Isotype
IgG
Related Products
Description
- The immunogen is 100% (17/17) homologous to SARS-COV-2 (COVID-19) Nucleocapsid protein
- The cross reactivity is not empirically tested
- Suggested positive control: transfected mouse melanoma cell lysate
- Severe Acute Respiratory Syndrome (SARS), an emerging disease characterized by atypical pneumonia, has recently been attributed to a novel coronavirus (SARS-CoV)
- The nucleocapsid protein (N) was one of the structural proteins of SARS-CoV (N, S, sE, M)
- The severe acute respiratory syndrome coronavirus (SARS-CoV) nucleocapsid (N) protein is the most abundant protein in the virus-infected cells
- The SARS-CoV-2 S gene has 76% amino acid similarity to the SARS-CoV S gene, and nonsynonymous mutations developed in the S protein as the SARS-CoV epidemic developed, reports have shown that the crystal structure of the SARS-CoV-2 nucleocapsid protein is similar to those of previously described coronavirus N proteins, but their surface electrostatic potential characteristics are distinct.