MABN361MI

MilliporeSigma™ Mouse anti-VAPA, Clone: 7E10.1,

Manufacturer: MilliporeSigma™

Select a Size

Pack Size SKU Availability Price
Each of 1 MABN361MI-Each-of-1 In Stock ₹ 40,292.08

MABN361MI - Each of 1

₹ 40,292.08

In Stock

Quantity

1

Base Price: ₹ 40,292.08

GST (18%): ₹ 7,252.574

Total Price: ₹ 47,544.654

Antigen

VAPA

Classification

Monoclonal

Formulation

Purified mouse monoclonal IgG1κ antibody in buffer containing 0.1M Tris-Glycine (pH 7.4), 150mM NaCl with 0.05% sodium azide.

Gene Symbols

VAPA; VAP33

Immunogen

GST-tagged recombinant protein corresponding to the C-terminal half of human VAPA.

Quantity

100 μg

Research Discipline

Neuroscience

Gene ID (Entrez)

NP_919415

Content And Storage

Stable for one year at 2°C to 8°C from date of receipt.

Isotype

IgG1 κ

Applications

Immunohistochemistry (Paraffin), Western Blot

Clone

7E10.1

Gene Accession No.

Q9P0L0

Host Species

Mouse

Purification Method

Protein G Purified

Regulatory Status

RUO

Primary or Secondary

Primary

Target Species

Human, Mouse

Form

Purified

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Description

  • Specifically detects VAPA clone: 7E10.1 in Human, Mouse samples, and it is validated for Immunohistochemistry (Paraffin), Western Blotting Vesicle-associated membrane protein-associated protein A (UniProt Q9P0L0; also known as 33kDa VAMP-associated protein, hVAP-33, VAMP-A, VAMP-associated protein A, VAP-33, VAP-A) is encoded by the VAPA (also known as VAP33) gene (Gene ID 9218) in human
  • VAMP-associated proteins (VAPs) are type IV membrane proteins that are well conserved among species
  • There exist three human VAPs encoded by two genes, with VAPA encoding VAP-A and VAPB encoding VAP-B and VAP-C
  • VAPs generally localize at the endoplasmic reticulum (ER), although they are also reported to localize at other subcellular organelles in some species and cell types
  • VAP-A contains a major sperm protein (MSP) domain at the N-terminal, followed by a coiled-coil domain, and a transmembrane (TM) domain
  • VAPs were shown to have important roles in non-vesicular lipid transport, lipid metabolism, the regulation of ER structure, and the unfolded protein response through MSP domain-mediated interaction with FFAT motifs
  • Oxysterol-binding protein (OSBP) is a cytosolic receptor of cholesterol and oxysterols
  • OSBP is recruited to the ER by binding to the MSP domain of VAP-A, a process essential for the stimulation of sphingomyelin synthesis by 25-hydroxycholesterol.