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Recombinant Human PDGFB

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Product Source Size Cat. No. Price
Recombinant Human PDGFB E. coli10 µg Z100355 $70.00
500 µg Z100357 $600.00
1.0 mg Z100359 $1,100.00
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Data Sheet
Print Version
Alternative Names PDGF subunit B, PDGF-2, Platelet-derived growth factor B chain, Platelet-derived growth factor beta polypeptide, Proto-oncogene c-Sis, PDGF-BB
Recombinant Human Platelet-Derived Growth Factor Subunit B (PDGFB)
Description The PDGF family is comprised of five different disulphide-linked dimers of four different polypeptide chains: A, B, C and D (PDGF-AA, PDGF-BB, PDGF-AB, PDGF-CC and PDGF-DD). Synthesized mainly by megakaryocytes, PDGFs are stored in the alpha granules of platelets from which they are released following platelet activation. Functioning as an autocrine and paracrine growth factor, PDGFs are involved in a number of biological processes that include but not limited to hyperplasia, chemotaxis, embryonic neuron development, wound healing and respiratory tubule epithelial cell development. Aberrant expression of PDGFs is observed with vascular proliferative diseases such as atherosclerosis. PDGFs regulate the synthesis of their own receptor and also influence the expression of membrane receptors for IL1, EGF, 5-Hydroxytryptamine, LDL and transferrin. Recombinant human PDGFB is a disulfide-linked homodimer of two B chains.
Gene Symbol PDGFB
Gene ID 5155
Accession No. P01127
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 12.3 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method
Purity >95% as determined by SDS-PAGE
Gel Image Click To Enlarge
Bioactivity The ED50 as determined by the dose-dependent proliferation of NIH 3T3 cells is <0.5ng/ml
Bioactivity Data Click To Enlarge
Formulation Lyophilized from a 0.2 μm filtered solution in PBS
Reconstitution A quick spin of the vial followed by reconstitution in sterile distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
Storage The lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
Usage For research use only. Not for diagnostic or therapeutic use.
Product Documents
Product References
FAQs
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How are endotoxin levels measured?
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970.

· Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL).

· For recombinant proteins: EU is reported per microgram of protein.

· One EU = 0.1-0.2 ng endotoxin/µg of protein.

· At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.