HCC-1 Human Recombinant ( CCL14 ) ( HCC 1 Human )

Catalog # PT_40844

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$201.00
DescriptionHCC-1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 8411 Dalton. The HCC-1 is purified by proprietary chromatographic
Product Size: 2ug
Quantity

Data sheet

Formulation
The CCL14 protein was lyophilized with 20mM PBS pH-7.4 and 150mM NaCl.
Solubility
It is recommended to reconstitute the lyophilized HCC-1 in sterile 18M-cm H2O not less than 100ug/ml, which can then be further diluted to other aqueous solutions.
Purity
Greater than 97.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Description
HCC-1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 8411 Dalton. The HCC-1 is purified by proprietary chromatographic techniques.
Protein Background
Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that
Expression host
Escherichia Coli.
Synonyms
Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.
Reagent Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized HCC1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL14 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a c
Amino acid sequence
TESSSRGPYHPSECCFTYTTYKIPRQRIMDYYETNSQCSKPGIVFITKRGHSVCTNPSDKWVQDYIKDMKEN.
Biological Activity
The Biological activity is calculated by its ability to chemoattract Human monocytes at 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.
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