Recombinant Human Semaphorin 3G Fc Chimera Protein, CF
Recombinant Human Semaphorin 3G Fc Chimera Protein, CF Summary
Product Specifications
The ED50 for this effect is 100-600 ng/mL.
Human Semaphorin 3G (Gly23-Thr782)(R557S, R558S, R560S, R561S, R774S, R777S) Accession # Q9NS98.1 | IEGRMD | Human IgG1 (Pro100-Lys330) |
N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
10804-S3
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
Recombinant Human Semaphorin 3G Fc Chimera inhibits the proliferation of HUVEC human umbilical vein endothelial cells. The ED50 for this effect is 100-600 ng/mL.
Reconstitution Calculator
Background: Semaphorin 3G
Semaphorin 3G (Sema3G), also known as Semaphorin sem2, is a class 3 member of the semaphorin family initially identified as regulators of neuron-axonal guidance (1, 2). More than 30 semaphorins have been discovered and are divided into eight classes: classes 1 and 4–7 are membrane-associated, while classes 2, 3, and 8 are in a secreted form (1, 2). Mature human Sema3G consists of an N-terminal sema domain, a plexin-semaphorin-integrin (PSI) domain, an Ig-like C2-type domain and a C-terminal basic domain (3). Within the extracellular domain, human Sema3G shares 87% amino acid sequence identity with mouse and rat Sema3G. In vitro analysis shows Sema 3G binds to Neuropilin-2, which forms a receptor complex with Plexin-D1. Via this pathways Sema 3G controls lymphatic vascular patterning by the means of cellular collapse (4). It shows protective effects in ischemic retinopathies by coordinating interactions of beta -catenin and VE-Cadherin in endothelium (5). Sema 3G has been shown to be involved in adipocyte differentiation. Knockdown of Sema3G inhibited weight gain through PI3K/Akt/GSK3 beta signaling in the adipose tissue and the AMPK/SREBP-1c pathway in the liver. Thus, Sema 3G is an adipokine essential for adipogenesis, lipogenesis, and insulin resistance and is associated with obesity (6).
- Alto, L.T. and Terman, J.R. (2017) Methods Mol. Biol. 1493:1.
- Jackson, R.E. and Eickholt, B.J. (2009) Curr. Biol. 19:R504.
- Toledano S. et al. (2019) J. Mol. Sci. 20:556.
- Liu, X. et al. (2016) Cell Rep. 17:2299.
- Chen, D. et al. (2021) J. Clin. Invest. 131:e135296.
- Liu, M. et al. (2020) J. Endocrinol. 244:223.
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