Sf9, Baculovirus cells.
Neural cell adhesion molecule 1, Neural cell adhesion molecule 1 isoform3, N-CAM-1, NCAM-1, CD56, NCAM1, NCAM, MSK39
Sterile filtered colorless solution.
Greater than 95.0% as determined by SDS-PAGE.
NCAM1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 593 amino acids (20-603 a.a) and having a molecular mass of 65.7kDa.
NCAM1 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Neural Cell Adhesion Molecule 1 (NCAM1), a member of the immunoglobulin superfamily, plays a crucial role in various neuronal processes. NCAM1 exhibits specific binding affinity, contributing to neurite fasciculation, neuron-to-neuron adhesion, and neurite outgrowth. Notably, the polysialylation of NCAM1 diminishes its adhesive properties while augmenting its ability to promote neurite outgrowth. Primarily expressed in NK cells and a subset of T lymphocytes, NCAM1 participates in MHC-unrestricted cell-mediated cytotoxicity. The elevated expression of NCAM1 serves as a marker of activated NK cells. During hematopoiesis, NCAM1 acts as a prototypical marker for NK cells and is also found on a subset of CD4+, CD8+, and T cells. Furthermore, NCAM1 contributes to cell-cell adhesion during embryonic development.
Recombinant human NCAM1, expressed in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It comprises 593 amino acids (20-603 a.a), resulting in a molecular weight of 65.7 kDa. This protein includes a 6-amino acid His-tag fused at the C-terminus and is purified using proprietary chromatographic methods.
Sterile filtered, colorless solution.
The NCAM1 solution is provided at a concentration of 1 mg/ml and is formulated in Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol.
For short-term storage (up to 2-4 weeks), the entire vial can be stored at 4°C. For extended storage, freezing at -20°C is recommended. To further enhance stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is advisable. It is crucial to avoid repeated freeze-thaw cycles to maintain protein integrity.
The purity of NCAM1 is greater than 95.0%, as determined by SDS-PAGE analysis.
Neural cell adhesion molecule 1, Neural cell adhesion molecule 1 isoform3, N-CAM-1, NCAM-1, CD56, NCAM1, NCAM, MSK39
Sf9, Baculovirus cells.
ADPLQVDIVP SQGEISVGES KFFLCQVAGD AKDKDISWFS PNGEKLTPNQ QRISVVWNDD SSSTLTIYNA NIDDAGIYKC VVTGEDGSES EATVNVKIFQ KLMFKNAPTP QEFREGEDAV IVCDVVSSLP PTIIWKHKGR DVILKKDVRF IVLSNNYLQI RGIKKTDEGT YRCEGRILAR GEINFKDIQV IVNVPPTIQA RQNIVNATAN LGQSVTLVCD AEGFPEPTMS WTKDGEQIEQ EEDDEKYIFS DDSSQLTIKK VDKNDEAEYI CIAENKAGEQ DATIHLKVFA KPKITYVENQ TAMELEEQVT LTCEASGDPI PSITWRTSTR NISSEEKTLD GHMVVRSHAR VSSLTLKSIQ YTDAGEYICT ASNTIGQDSQ SMYLEVQYAP KLQGPVAVYT WEGNQVNITC EVFAYPSATI SWFRDGQLLP SSNYSNIKIY NTPSASYLEV TPDSENDFGN YNCTAVNRIG QESLEFILVQ ADTPSSPSID QVEPYSSTAQ VQFDEPEATG GVPILKYKAE WRAVGEEVWH SKWYDAKEAS MEGIVTIVGL KPETTYAVRL AALNGKGLGE ISAASEFKTQ PVHSPPPHHH HHH
NCAM1 is a homophilic binding glycoprotein expressed on the surface of neurons, glia, and skeletal muscle . It has three main isoforms, which differ in their cytoplasmic domains:
The extracellular domain of NCAM1 consists of five immunoglobulin-like (Ig) domains followed by two fibronectin type III (FNIII) domains . These domains are involved in homophilic binding and signaling leading to neurite outgrowth.
NCAM1 is involved in various biological processes, including:
Additionally, NCAM1 interacts with fibroblast growth factor receptors, N-cadherin, and other components of the extracellular matrix, triggering signaling cascades involving FYN-focal adhesion kinase (FAK), mitogen-activated protein kinase (MAPK), and phosphatidylinositol 3-kinase (PI3K) .
NCAM1 is implicated in several medical conditions:
Recombinant NCAM1 is produced in various systems, including Sf9 Baculovirus cells. It is a single, glycosylated polypeptide chain containing 593 amino acids and has a molecular mass of approximately 65.7kDa . This recombinant protein is often used in research to study its functions and interactions.