WD Repeat Domain Phosphoinositide-Interacting Protein 1 (WIPI1) Antibody

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Description
WIPI1 Antibody is a Rabbit Polyclonal 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 |
Recommended Dilution | WB: 1/500 - 1/2000, IHC: 1/20 - 1/200. Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purification | Antigen Affinity Chromatography. |
Size 1 | 20 µl |
Size 2 | 50 µl |
Size 3 | 100 µl |
Size 4 | 200 µl |
Size 5 | 1 ml |
Form | Liquid |
Tested Applications | ELISA, WB, IHC |
Buffer | PBS, pH 7.3, containing 0.02% sodium azide and 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_001307701.1, NM_001320772.1, NP_060453.3, NM_017983.6 |
OMIM | 609224 |
Background | Antibody anti-WIPI1 |
Status | RUO |
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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