Anti-RLTPR Purified CARMIL2 Monoclonal Antibody

Boster Bio Anti-RLTPR Purified CARMIL2 Monoclonal Antibody (Catalog# M10789) . Tested in Flow Cytometry, WB application (s) . This antibody reacts with Mouse, Human.

Product Specifications

Background

RLTPR / CARMIL2 (RGD motif, leucine rich repeats, tropomodulin domain and proline-rich containing; capping protein regulator and myosin 1 linker 2), also known as LRRC16C, is a cytosolic protein, which with high affinity binds CAPZA2 (capping protein muscle actin Z-line alpha 2) and decreases CAPZA2 affinity for actin barbed ends. RLTPR / CARMIL2 increases the rate of actin filament elongation from seeds in the presence of CAPZA2, however, seems unable to nucleate filaments. Its interaction with CAPZA2 is essential for lamellipodial protrusion and cell translocation. RLTPR / CARMIL2 is crutial for T cell costimulation via CD28 and this property seems to be independent on its actin-uncapping function. The lack of functional RLTPR / CARMIL2 molecules impeded the differentiation toward Th1 and Th17 fates of both human and murine CD4+ T cells and leads to combined immunodeficiency. Expression of RLTPR / CARMIL2 was also detected in human and murine B cells, but it seems not to be involved in BCR-mediated signaling.

Synonyms

CARMIL2, LRRC16C

Gene Name

CARMIL2

UniProt

Q6F5E8

Host

Mouse

Reactivity

Mouse, Human

Immunogen

Murine RLTPR. The mouse monoclonal antibody EM-53 recognizes RLTPR / CARMIL2, an intracellular protein playing a role in actin filament elongation.

Clonality

Monoclonal

Clone

Clone: EM-53

Tissue Specificity

Expressed in all tissues tested, including thymus, spleen, colon, leukocytes, peripheral blood, skin, skin keratinocytes and skin fibroblasts.

Applications

Flow Cytometry, WB

Purification

Purified by protein-A affinity chromatography.

Concentration

1 mg/ml

Dilution

Flow cytometry: 1-4 µg/ml. Intracellular staining.

Form

Liquid

Function

Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization (PubMed:26466680) . Plays a role in cell protrusion formations; involved in cell polarity, lamellipodial assembly, membrane ruffling and macropinosome formations (PubMed:19846667, PubMed:26578515, PubMed:26466680) . Involved as well in cell migration and invadopodia formation during wound healing (PubMed:19846667, PubMed:26578515, PubMed:26466680) .