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Recombinant Human CCL4

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Product Source Size Cat. No. Price
Recombinant Human CCL4 E. coli10 µg Z100685 $70.00
100 µg Z100687 $325.00
1.0 mg Z100689 $1,690.00
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Data Sheet
Print Version
Alternative Names C-C motif chemokine 4, G-26, T-lymphocyte-secreted protein HC21, Lymphocyte activation gene 1 protein, LAG-1, MIP-1-beta(1-69), MIP-1-beta, PAT 744, Protein H400, SIS-gamma, Small-inducible cytokine A4, T-cell activation protein 2, ACT-2, MIP1B, SCYA4
Recombinant Human Macrophage Inflammatory Protein-1 Beta (CCL4)
Description Macrophage Inflammatory Protein-1 is a factor produced by macrophages that causes local inflammatory responses, and induces superoxide production by neutrophils. Two peptides are responsible for this activity. They have been termed MIP-1-alpha, and MIP-1-beta. The two MIP proteins are the major factors produced by macrophages following their stimulation with bacterial endotoxins. Both proteins are involved in the cell activation of human granulocytes (neutrophils, eosinophils, and basophils) and appear to be involved in acute neutrophilic inflammation. Both forms of MIP-1 stimulate the production of reactive oxygen species in neutrophils and the release of lysosomal enzymes. They also induce the synthesis of other pro-inflammatory cytokines such as IL-1, IL-6 and TNF in fibroblasts and macrophages. MIP-1-alpha is a potent agonist of basophils, inducing a rapid change of cytosolic free calcium (see also: Calcium ionophore), the release of histamine and sulfido- leukotrienes, and Chemotaxis. Murine MIP-1- alpha is the primary stimulator of TNF secretion by macrophages, whereas MIP-1-beta antagonizes the inductive effects of MIP-1- alpha. In human monocytes the production of MIP-1-beta can be induced by bacterial lipopolysaccharides and IL-7. The biological activities of MIP-1-alpha and MIP-1-beta are mediated by receptors that bind both factors CCR5. A second species of receptors for these two factors also appears to bind MCAF.
Gene Symbol CCL4
Gene ID 6351
Accession No. P13236
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 8.0 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 ED(50) was determined by the dose-dependent proliferation of KMS15 cells and was found to be <0.2ng/mL.
Bioactivity Data Click To Enlarge
Formulation Recombinant MIP-1 beta was lyophilized from a 0.2 μm filtered PBS solution.
Reconstitution A quick spin of the vial followed by reconstitution in 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.