Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine NFS?60 cells is less than 0.05 ng/ml, corresponding to a specific activity of >2.0x107 IU/mg.
Lyophilized from a 0.2 m filtered 10 mM Sodium Citrate, pH 4.0, 150 mM NaCl, 0.01 % Tween20
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature
and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized
form is 12 months at -20°C/-80°C.
5-10 business days
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
I purchased CSB-AP003161MO Granulocyte colony-stimulating factor protein(Csf3) (Active). The lot is 03793. How to dissolve the lyophilized protein?
Very nice to receive your inquiry. Regarding how to dissolve the lyophilized protein of CSB-AP003161MO, pls check the reply from our technical department as follows: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.
Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.
Gene References into Functions
We confirmed that acute lung injury was associated with high serum G-CSF levels, and elevated neutrophil elastase activity in the lungs and serum of mice with adenine-induced acute kidney injury (AKI). G-CSF could be a target for new anti-lung injury strategy in patients with AKI. PMID:
The opposing roles of G-CSF and IFNgamma in regulation of innate inflammatory responses in a murine viral encephalitis model reveal G-CSF as a potential therapeutic target. PMID:
central regulator of the transition to postinflammatory chronic visceral pain PMID:
We propose that in aggressive pancreatic ductal adenocarcinoma , elevated G-CSF contributes to tumor progression through promoting increases in infiltration of neutrophil-like cells with high immunosuppressive activity. Such a mechanism provides an avenue for a neoadjuvant therapeutic approach for this devastating disease PMID:
these data provide strong evidence for a role for G-CSF in the development of ACI after burn injury through suppression of EPO signaling in bone marrow erythroid cells. PMID:
physiologically produced G-CSF not only acts as a neutrophil mobilizer at the relatively late stage of acute inflammation, but also prevents exaggerated neutrophil mobilization. PMID:
data demonstrate that G-CSF is a pivotal driver of the disease progression in the K/BxN serum-transfer arthritis (STA) model and possibly acts in part by regulating neutrophil numbers in the circulation PMID:
SB203580 increases G-CSF expression in macrophages by increasing the stability of G-CSF mRNA via its 3'UTR, and the effect was not due to its inhibition of p38 MAPK activity. PMID:
Results suggested that G-CSF plays an important role in preventing colitis, likely through populating immune regulatory macrophages in the intestine. PMID:
findings provide convincing evidence that monophosphoryl lipid A-induced G-CSF facilitates early expansion, mobilization, and recruitment of neutrophils to the site of infection after burn injury PMID:
Overexpression of VEGF may compensate for the G-CSF deficit through preservation of cellular components, including blood vessels, in the postinfarction heart. PMID:
rapidly induces autophagy after spinal cord injury to inhibit neuronal apoptosis PMID:
G-CSF supports long-term muscle regeneration in mouse models of muscular dystrophy. PMID:
constitutive activation of the NF-kappaB pathway in CAIX-depleted cells restored G-CSF secretion PMID:
Exposure of Sca-1(+) cells to G-CSF in the culture medium for 72 h induced time-dependent but self-limiting cell cycle acceleration with a restricted effect on the CSC proliferation. PMID:
these results suggest that the G-CSF pathway regulates the production of autoantibodies in murine models of lupus. PMID:
G-CSF acts in a cell intrinsic manner to expand multipotent progenitors to increase production of tumor-derived Ly6G+ neutrophils. PMID:
Endothelial cell(EC)-intrinsic MYD88 signaling and subsequent G-CSF production by ECs is required for myeloid progenitor lineage skewing toward granulocyte-macrophage progenitors, increased colony-forming unit granulocyte activity. PMID:
Adventitial CXCL1/granulocyte-colony stimulating factor expression in response to aortic dissection triggers local neutrophil recruitment and activation. This leads to adventitial inflammation via IL-6 and results in aortic expansion and rupture. PMID:
Cultured mouse enteric nervous system -neurospheres show increased expansion with increased G-CSF concentrations, in contrast to central nervous system - derived spheres. PMID:
G-CSF STAT3 axis constitutes a key protective mechanism induced by injury to reduce the risk for posttraumatic infection. PMID:
After deletion of Pten in mice lacking G-CSF, the splenomegaly, myeloproliferative disease, and splenic hematopoietic stem cell accumulation are rescued. PMID:
Our results suggest 5-AED survival enhancement is G-CSF-dependent, and that it stimulates innate immune cell function and reduces radiation-induced DNA damage via induction of genes that modulate cell cycle progression and apoptosis. PMID:
activation of the RAS/MEK/ERK pathway regulates G-CSF expression through the Ets transcription factor PMID:
G-CSF protein is necessary and sufficient to restore monocyte chemoattractant protein (MCP)-1 deficiency in neutrophil-mediated host immunity following Klebsiella pneumoniae lung infection. PMID:
Ang2 deficiency results in enhanced recruitment of myeloid cells depending on G-CSF, and that the enhancement results in more aggressive tumor growth and neo-angiogenesis during liver colonization. PMID:
Il-1rn knockout mice exhibit delayed resolution in acute lung inflammation after exposure to lipopolysaccharide, a process that appears to be mediated via the granulocyte colony-stimulating factor/IL-17A axis. PMID:
Induction of Bv8 expression by granulocyte colony-stimulating factor in CD11b+Gr1+ cells: key role of Stat3 signaling. PMID:
BMMCs and G-CSF co-administration exhibits synergistic beneficial effect over time. PMID:
granulocyte and macrophage populations of murine bone marrow cells are regulated by G-CSF and CD137 protein PMID:
TLR2 signaling in G-CSF mobilized PBSCs correlates with their ability to rapidly differentiate into myeloid cells, resulting in improved engraftment PMID:
G-CSF is crucial for skeletal myocyte development and regeneration PMID:
G-CSF and IL-6 provide signals that determine the angiogenic potential of BM resident monocytes. PMID:
G-CSF stimulates the expression of the MIP-2 receptor via STAT3-dependent transcriptional activation of Il8rb PMID:
G-CSF exerts potent anti-apoptotic activities towards motoneurons in vivo and suggests that the protection offered by G-CSF in ALS mouse models is due to its direct neuroprotective activity PMID:
Overexpression of STAT3beta did not alter the kinetics of G-CSF-mediated neutrophilic differentiation or p27 induction in 32D/G-CSF-R WT cells. PMID:
Increased production of G-CSF in mice mounting the acute phase response is a key physiological component of host defense. PMID:
Evaluation of role of G-CSF in the production, survival, and release of neutrophils from bone marrow into circulation using G-CSF-deficient mice PMID:
G-CSF induces neutrophil mobilization indirectly through the generation of trans-acting signals PMID:
G-CSF mediates granulopoiesis and, as a corollary, participates in neutrophilia in LFA-1 deficient mice. PMID:
regulation of G-CSF levels may provide a mechanism for directing primitive hematopoietic progenitors into the common myeloid lineage in response to environmental stresses PMID:
G-CSF treatment leads to Lyn-mediated tyrosine phosphorylation of Gab2, which may serve as an important intermediate of enhanced Akt activity and myeloid differentiation, not growth/survival response. PMID:
G-CSF signaling in neutrophils is negatively regulated by SOCS3 PMID:
observations show that lipocalin 24p3 is not involved in the granulocyte-colony stimulating factor withdrawal-induced apoptosis PMID:
critical role for G-CSF in driving joint inflammation and as a potential therapeutic target in inflammatory joint diseases, such as rheumatoid arthritis. PMID:
G-CSF induces stabilization of Fli-1 protein in myeloid cells PMID:
G-CSF treatment significantly improved survival and liver histology in chemically injured mice, predominantly by promoting endogenous repair mechanisms; immunohistochemistry showed a higher percentage of bone marrow-origin hepatocytes PMID:
Febrile-range hyperthermia-induced expression of G-CSF drives the sustained peripheral neutrophilia that occurs during sustained (36 h) hyperthermia in a conscious temperature-clamped mouse model. PMID:
G-CSF modulates angiogenesis by increasing myelomonocytic cells (VEGFR1+ neutrophils) and their release of VEGF PMID:
monocytes mobilized into the blood by G-CSF or AMD3100 stimulate angiogenesis at sites of ischemia through a paracrine mechanism PMID: