LRRC8A Antibody

Product Specifications

Background

The leucine rich repeat containing 8 family member A protein (LRRC8A) belongs the LRRC8 family of proteins within the LRR superfamily of proteins, which are involved in diverse biological processes, including cell adhesion, cellular trafficking, and hormone-receptor interactions (1,2) . LRRC8A is a four-pass transmembrane protein that plays a role in B cell development. Defects in this gene cause autosomal dominant non-Bruton type agammaglobulinemia, an immunodeficiency disease resulting from defects in B cell maturation (1) . LRRC8A has also been shown to be an essential component of the volume-regulated anion channel VRAC (3) .

NCBI Gene ID

56262

Swiss Prot

Q8IWT6

Accession Number

NP_062540

Host

Rabbit

Reactivity

Human, Mouse, Rat

Clonality

Polyclonal

Conjugation

Unconjugated

Type

Primary Antibodies

Field of Research

Stem Cell, Signal Transduction

Purification

LRRC8A antibody is affinity chromatography purified via peptide column.

Positive Control

Cat. No. 1287 - EL4 Cell Lysate

Concentration

1 mg/mL

Buffer

LRRC8A antibody is supplied in PBS containing 0.02% sodium azide.

Modification

None

Shipping Conditions

Blue Ice

Storage Conditions

LRRC8A antibody can be stored at 4˚ C for three months and -20˚ C, stable for up to one year.

Observed Molecular Weight

Multiple other LRRC8A antibodies also show a ~95kD band

Fragment

IgG

Specificity

LRRC8A antibody is human, mouse and rat reactive.

Symbol

LRRC8A

NCBI Official Name

Leucine rich repeat containing 8 family, member A

NCBI Organism

Homo sapiens

Background Reference 01

Sawada A, Takihara Y, Kim JY, et al. A congenital mutation of the novel gene LRRC8 causes agammaglobulinemia in humans. J. Clin. Invest. 2003; 112:1707-13.

Background Reference 02

Kubota K, Kim JY, Sawada A, et al. LRRC8 involved in B cell development belongs to a novel family of leucine-rich repeat proteins. FEBS Lett. 2004; 564:147-52.

Background Reference 03

Voss FK, Ullrich F, Munch J, et al. Identification of LRRC8 heteromers as an essential component of the volume-regulated anion channel VRAC. Science 2014; 344:634-8.