WD Repeat Domain Phosphoinositide-Interacting Protein 1 (WIPI1) Antibody
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Description
WIPI1 Antibody is a Rabbit Polyclonal Antibody against WIPI1.
Documents del producto
Product specifications
| Category | Primary Antibodies |
| Immunogen Target | WD Repeat Domain Phosphoinositide-Interacting Protein 1 (WIPI1) |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Recommended Dilution | ELISA: 1 µg/ml, WB: 1/500 - 1/2000. Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Unconjugated |
| Isotype | IgG |
| Purification | Purified by affinity chromatography. |
| Size 1 | 20 µl |
| Size 2 | 100 µl |
| Size 3 | 2 × 100 µl |
| Form | Liquid |
| Tested Applications | ELISA, WB |
| Buffer | PBS, pH 7.3, containing 0.02% sodium azide, 50% glycerol. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | Q5MNZ9 |
| Gene ID | 55062 |
| NCBI Accession | NP_060453.3 |
| Background | Antibody anti-WIPI1 |
| Status | RUO |
| Note | Concentration: > 0.2 mg/ml - |
Descripción
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WIPI1 antibody
This gene encodes a WD40 repeat protein. Members of the WD40 repeat family are key components of many essential biologic functions. They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein-protein interactions. Members of the WIPI subfamily of WD40 repeat proteins have a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids. Alternative splicing results in multiple transcript variants.
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WIPI1 Antibody is a Rabbit Polyclonal Antibody against WIPI1.
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WD40 repeat proteins are key components of many essential biologic functions. They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible protein-protein interactions. Members of the WIPI subfamily of WD40 repeat proteins, such as WIPI1, have a 7-bladed propeller structure and contain a conserved motif for interaction with phospholipids (Proikas-Cezanne et al., 2004 [PubMed 15602573]).
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