FLRT2 Human
Sf9, Baculovirus cells.
Leucine-rich repeat transmembrane protein FLRT2, Fibronectin-like domain-containing leucine-rich transmembrane protein 2, KIAA0405, UNQ232/PRO265.
Greater than 90.0% as determined by SDS-PAGE.
Description
FLRT2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 514 amino acids (36-541 a.a) and having a molecular mass of 57.5kDa.
FLRT2 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Product Specs
Fibronectin Leucine Rich Transmembrane Protein 2 (FLRT2) is a glycoprotein that belongs to the family of FLRT glycoproteins (fibronectin, leucine rich repeat, transmembrane). It is primarily found in specific regions of the brain and other tissues. The extracellular domain of FLRT2 shares approximately 47% similarity with FLRT1 and FLRT3. All three FLRT proteins contain a fibronectin domain that can bind to epidermal growth factor receptors.
Recombinant human FLRT2, expressed in Sf9 insect cells using a baculovirus system, is a single, glycosylated polypeptide chain. This protein consists of 514 amino acids (with residues 36-541 present) and has a molecular weight of 57.5 kDa. It includes an 8 amino acid His-tag fused to the C-terminus. Purification is achieved through proprietary chromatographic methods.
The FLRT2 solution is provided at a concentration of 0.25 mg/mL in a buffer containing 10% glycerol and Phosphate-Buffered Saline (PBS) at a pH of 7.4.
For short-term storage (up to 2-4 weeks), the FLRT2 solution should be kept at 4°C. For long-term storage, it is recommended to store the solution at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is advisable for extended storage periods. Repeated freezing and thawing should be avoided.
The purity of FLRT2 is determined to be greater than 90% using SDS-PAGE analysis.
Leucine-rich repeat transmembrane protein FLRT2, Fibronectin-like domain-containing leucine-rich transmembrane protein 2, KIAA0405, UNQ232/PRO265.
Sf9, Baculovirus cells.
CPSVCRCDRN FVYCNERSLT SVPLGIPEGV TVLYLHNNQI NNAGFPAELH NVQSVHTVYL YGNQLDEFPM NLPKNVRVLH LQENNIQTIS RAALAQLLKL EELHLDDNSI STVGVEDGAF REAISLKLLF LSKNHLSSVP VGLPVDLQEL RVDENRIAVI SDMAFQNLTS LERLIVDGNL LTNKGIAEGT FSHLTKLKEF SIVRNSLSHP PPDLPGTHLI RLYLQDNQIN HIPLTAFSNL RKLERLDISN NQLRMLTQGV FDNLSNLKQL TARNNPWFCD CSIKWVTEWL KYIPSSLNVR GFMCQGPEQV RGMAVRELNM NLLSCPTTTP GLPLFTPAPS TASPTTQPPT LSIPNPSRSY TPPTPTTSKL PTIPDWDGRE RVTPPISERI QLSIHFVNDT SIQVSWLSLF TVMAYKLTWV KMGHSLVGGI VQERIVSGEK QHLSLVNLEP RSTYRICLVP LDAFNYRAVE DTICSEATTH ASYLNNGSNT ASSHEQTTSH SMGSPFLEHH HHHH
Product Science Overview
FLRT2 is a type I transmembrane protein characterized by an extracellular region that includes an N-terminal leucine-rich repeat domain and a type 3 fibronectin domain. This is followed by a transmembrane domain and a short C-terminal cytoplasmic tail domain . The extracellular region is essential for its interaction with other proteins and its role in cell signaling.
FLRT2 is expressed in various tissues, with significant roles in early embryonic vascular and neural development . It is almost undetectable in human monocytic cell lines, human peripheral blood mononuclear cells (PBMCs), and mouse primary monocytes but significantly increases in fully differentiated macrophages .
FLRT2 functions as both a homophilic cell adhesion molecule and a heterophilic chemorepellent. It mediates cell-cell adhesion via interactions with ADGRL3 and other latrophilins expressed on adjacent cells . Additionally, FLRT2 plays a role in the migration of cortical neurons during brain development through its interaction with UNC5D . It also mediates axon growth cone collapse and acts as a repulsive guidance cue for neurons .
The expression and function of FLRT2 are regulated through proteolytic removal of its extracellular region, which controls the migration of neurons in the developing cortex . Additionally, myeloid-specific deletion of FLRT2 in mice leads to decreased monocyte-to-macrophage generation and impaired macrophage functions .
