Recombinant Mouse PDGF-C Protein (Fc Tag)

Name: Recombinant Mouse PDGF-C Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-3718
Availability: InStock

Collections: Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Tag	Fc
Host Species	Mouse
Accession	Q8CI19
Synonym	1110064L01Rik, AI647969, PDGF-C
Background	PDGF-C is a member of the PDGF/VEGF family of growth factors with a unique domain organization and expression pattern. Platelet-derived growth factor receptors (PDGFRs) are catalytic receptors that have intracellular tyrosine kinase activity. They have roles in the regulation of many biological processes including embryonic development, angiogenesis, cell proliferation and differentiation, and contribute to the pathophysiology of some diseases, including cancer. There are two isoforms of the PDGFR receptor; PDGFRalpha and PDGFRbeta, which can form homo- or heterodimers. The endogenous PDGFR ligands are PDGF-A, -B, -C and -D, which induce receptor dimerization and transphosphorylation at specific tyrosine residues upon binding. This activates the intracellular kinase activity, initiating intracellular signaling through the MAPK, PI 3-K and PKCgamma pathways. PDGF-C acts as a specific ligand for alpha platelet-derived growth factor receptor homodimer, and alpha and beta heterodimer. Binding of this growth factor to its affinity receptor elicits a variety of cellular responses. PDGF-C Appears to be involved in the three stages of wound healing: inflammation, proliferation and remodeling. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs.
Description	A DNA sequence encoding the receptor-binding form of mouse PDGFC (Q8CI19) (Val 235-Gly 345) was fused with the Fc region of human IgG1 at the N-terminus.
Source	HEK293
Predicted N Terminal	Glu
AA Sequence	Val 235-Gly 345
Molecular Weight	The recombinant mouse PDGFC/Fc is a disulfide-linked homodimeric protein. The reduced monomer consists of 372 a.a. and has a predicted molecular mass of 40.9 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rmPDGFC/Fc monomer is approximately 46 kDa.
Purity	>80% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	1. Measured by its binding ability in a functional ELISA.2. Immobilized mouse PDGF-C at 10 ug/mL (100 ul/well) can bind- human PDGFRA, The EC50 of human PDGFRA is 0.71 ug/mL.3. Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells. The ED50 for this effect is typically 0.5-2 ug/mL.
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.