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The protein encoded by SYTL2 is a synaptotagmin-like protein (SLP) that belongs to a C2 domain-containing protein family. Zusätzlich bieten wir Ihnen SYTL2 Antikörper (22) und SYTL2 Kits (5) und viele weitere Produktgruppen zu diesem Protein an.
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Our findings indicate that Slp2-a controls renal cell size through regulation of Rap (zeige LRPAP1 Proteine)-ezrin (zeige EZR Proteine) signaling independently of Rab27 (zeige RAB27A Proteine).
Slp2-a is required for targeting of the signaling molecule podocalyxin (zeige PODXL Proteine) to the apical membrane in a Rab27A (zeige RAB27A Proteine)-dependent manner.
Calmodulin suppresses synaptotagmin-2 (zeige SYT2 Proteine) transcription in cortical neurons
Loss of Slp2-a protein also induced a change in melanocyte morphology, from their normal elongated shape to a more rounded shape, which depended on the phospholipid-binding activity of Slp2-a
Slp2-a is part of the mucin (zeige SLC13A2 Proteine) secretory machinery in surface mucous cells of mouse stomach
These results suggest that both Slp1 and Slp2-a may form part of a docking complex, capturing secretory lysosomes at the immunological synapse.
The structural characterization of the Rab27a (zeige RAB27A Proteine)-exophilin4/Slp2-a complex will clarify Rab27 (zeige RAB27A Proteine) recognition by its effectors prior to vesicle tethering and docking.
The observed structural complementation between the interacting surfaces of Rab27a (zeige RAB27A Proteine) and Exophilin4 sheds light on the disparities among the Rab27 (zeige RAB27A Proteine) effectors and outlines a general mechanism for their recruitment.[exophilin4]
Syt2 (zeige SYT2 Proteine) can serve as an exocytic sensor for diverse Ca(2 (zeige CA2 Proteine)+) signaling systems, and its levels are limiting for stimulated secretory function in airway goblet cells
Stress-induced mitochondrial hyperfusion (SIMH) is independent of MFN2, BAX/BAK, and prohibitins, but requires L-OPA1, MFN1, and the mitochondrial inner membrane protein SLP-2.
Overexpression of SYTL2 promoted metastatic potential.
SLP2 may play an important role in tumorigenesis of esophageal squamous cell carcinoma.
A high expression level of SLP-2 may be associating with the development of invasion and metastasis in laryngeal squamous cell carcinoma and breast cancer.
Exophilin4/Slp2-a is specifically expressed in pancreatic alpha cells.
Rab27a (zeige RAB27A Proteine) recruits Slp2a-hem on vesicular structures in peripheral CTLs and following CTL-target (zeige CTH Proteine) cell conjugate formation, the Slp2a-hem/Rab27a (zeige RAB27A Proteine) complex colocalizes with perforin (zeige PRF1 Proteine)-containing granules at the immunologic synapse
Rab27A/Slp2a expression in limb girdle muscular dystrophy 2B muscle provides a compensatory vesicular trafficking pathway that is able to repair membrane damage in the absence of dysferlin.
Synaptotagmin-like protein 2-a (Slp2-a) contains an N-terminal Slp (zeige SEPT9 Proteine) homology domain (SHD (zeige SHD Proteine)) (PMID: 11327731). The SHD (zeige SHD Proteine) of Slp2-a specifically and directly binds the GTP (zeige AK3 Proteine)-bound form of Rab27A (zeige RAB27A Proteine).
The protein encoded by this gene is a synaptotagmin-like protein (SLP) that belongs to a C2 domain-containing protein family. The SLP homology domain (SHD) of this protein has been shown to specifically bind the GTP-bound form of Ras-related protein Rab-27A (RAB27A). This protein plays a role in RAB27A-dependent vesicle trafficking and controls melanosome distribution in the cell periphery. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
, synaptotagmin-like protein 2
, breast cancer-associated antigen SGA-72M
, chromosome 11 synaptotagmin