
Thermo Fisher Scientific Human G-CSF Recombinant Protein, PeproTech
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Applications
Tested Dilution
Publications
Western Blot (WB)
Assay-dependent
View 1 publication 1 publication
ELISA (ELISA)
Assay-dependent
View 1 publication 1 publication
Functional Assay (Functional)
Assay-dependent
In vitro Assay (IV)
-
View 128 publications 128 publications
Miscellaneous PubMed (Misc)
-
View 15 publications 15 publications
Product Specifications
Species
Human
Published species
Human, Mouse, Non-human primate, Plant, Virus
Expression System
E. coli
Amino acid sequence
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL GHSLGIPWAP LSSCPSQALQ LAGCLSQLHS GLFLYQGLLQ ALEGISPELG PTLDTLQLDV ADFATTIWQQ MEELGMAPAL QPTQGAMPAF ASAFQRRAGG VLVASHLQSF LEVSYRVLRH LAQP
Molecular weight
18.7 kDa
Class
Recombinant
Type
Protein
Purity
≥ 98% by SDS-PAGE gel and HPLC analyses.
Endotoxin concentration
<1 EU/µg
Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of murine NFS-60 cells is ≤ 0.1 ng/ml, corresponding to a specific activity of ≥ 1 x 10^7 units/mg.
Conjugate
Unconjugated Unconjugated Unconjugated
Form
Lyophilized
Purification
purified
Contains
no preservative
Storage conditions
-20°C
Shipping conditions
Ambient
Product Specific Information
Recombinant Human G-CSF is an 18.7 kDa protein consisting of 174 amino acid residues.
This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis
Target Information
G-CSF (Granulocyte colony stimulating factor) is a naturally occurring cytokine that stimulates the production and antibacterial function of neutrophils and monocytes. Human G-CSF is an 18.8 kDa protein containing 175 amino acid residues, and a soluble isoform of the G-CSF receptor has been described. The pleotropic cytokine is produced by activated monocytes, macrophages, endothelial cells, fibroblasts, astrocytes, osteoblasts and bone marrow cells. G-CSF has been shown to have specific effects on the proliferation, differentiation and activation of hematopoietic cells. G-CSF is also expressed by various transformed cells such as carcinoma cells and myeloblastic leukemia cells. G-CSF is encoded by two distinct DNA sequences, resulting in a full size, high activity and a shorter, low activity isoform of G-CSF. G-CSF is highly conserved among species and has been shown to exert its biological functions through interaction with its receptor expressed on the surface of hematopoietic progenitors, neutrophilic granulocytes and certain carcinoma cell lines. Clinical use of G-CSF has been approved for several therapeutic applications, treatment of neonatal infections, therapy of acute myocardial infarction, granulocyte transfusion in patients with neutropenia, in severe infections and sepsis, therapy in chronic autoimmune neutropenia, treatment of acute myeloid leukemias, Sweet`s syndrome and AIDS. Further, G-CSF has been shown to be a marker protein for different carcinomas such as bladder cancer and dysfunction of the protein has been linked to Kostmann Syndrome.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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