Anti-SPTBN2 Antibody Picoband® Fluoro647 Conjugated

Spectrin beta chain, brain 2 is a protein that in humans is encoded by the SPTBN2 gene. Spectrins are principle components of a cell's membrane-cytoskeleton and are composed of two alpha and two beta spectrin subunits. The protein encoded by this gene (SPTBN2), is called spectrin beta non-erythrocytic 2 or beta-III spectrin. It is related to, but distinct from, the beta-II spectrin gene which is also known as spectrin beta non-erythrocytic 1 (SPTBN1) . SPTBN2 regulates the glutamate signaling pathway by stabilizing the glutamate transporter EAAT4 at the surface of the plasma membrane. Mutations in this gene cause a form of spinocerebellar ataxia, SCA5, that is characterized by neurodegeneration, progressive locomotor incoordination, dysarthria, and uncoordinated eye movements.

Atypical chemokine receptor 2; C-C chemokine receptor D6; Chemokine receptor CCR-10; Chemokine receptor CCR-9; Chemokine-binding protein 2; Chemokine-binding protein D6; ACKR2; CCBP2; CCR10; CMKBR9; D6

Found in endothelial cells lining afferent lymphatics in dermis and lymph nodes. Also found in lymph nodes subcapsular and medullary sinuses, tonsillar lymphatic sinuses and lymphatics in mucosa and submucosa of small and large intestine and appendix. Also found in some malignant vascular tumors. Expressed at high levels in Kaposi sarcoma-related pathologies. Expressed on apoptotic neutrophils (at protein level) . Expressed primarily in placenta and fetal liver, and found at very low levels in the lung and lymph node.

Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines including CCL2, CCL3, CCL3L1, CCL4, CCL5, CCL7, CCL8, CCL11, CCL13, CCL17, CCL22, CCL23, CCL24, SCYA2/MCP-1, SCY3/MIP-1-alpha, SCYA5/RANTES and SCYA7/MCP-3. Upon active ligand stimulation, activates a beta-arrestin 1 (ARRB1) -dependent, G protein-independent signaling pathway that results in the phosphorylation of the actin-binding protein cofilin (CFL1) through a RAC1-PAK1-LIMK1 signaling pathway. Activation of this pathway results in up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. By scavenging chemokines in tissues, on the surfaces of lymphatic vessels, and in placenta, plays an essential role in the resolution (termination) of the inflammatory response and in the regulation of adaptive immune responses. Plays a major role in the immune silencing of macrophages during the resolution of inflammation. Acts as a regulator of inflammatory leukocyte interactions with lymphatic endothelial cells (LECs) and is required for immature/mature dendritic cells discrimination by LECs.

1. Al-Muhaizea, M. A., AlMutairi, F., Almass, R., AlHarthi, S., Aldosary, M. S., Alsagob, M., AlOdaib, A., Colak, D., Kaya, N. A novel homozygous mutation in SPTBN2 leads to spinocerebellar ataxia in a consanguineous family: report of a new infantile-onset case and brief review of the literature. Cerebellum 17: 276-285, 2018. 2. Clarkson, Y. L., Gillespie, T., Perkins, E. M., Lyndon, A. R., Jackson, M. Beta-III spectrin mutation L253P associated with spinocerebellar ataxia type 5 interferes with binding to Arp1 and protein trafficking from the Golgi. Hum. Molec. Genet. 19: 3634-3641, 2010. 3. Clarkson, Y. L., Perkins, E. M., Cairncross, C. J., Lyndon, A. R., Skehel, P. A., Jackson, M. Beta-III spectrin underpins ankyrin R function in Purkinje cell dendritic trees: protein complex critical for sodium channel activity is impaired by SCA5-associated mutations. Hum. Molec. Genet. 23: 3875-3882, 2014.