Recombinant Human MIF His (C-Term) Protein

Novus Biologicals | Catalog # NBP2-35005

Novus Biologicals
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Key Product Details

Source

E. coli

Tag

His (C-Term)

Applications

Bioactivity, SDS-PAGE
View all MIF Proteins and Enzymes »

Product Specifications

Description

A single non-glycosylated polypeptide chain containing 117 amino acids corresponding to MIF with 6x His at the C-terminus Source: E. coli

Amino Acid Sequence: MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFALEHHH HHH

Purity

>95%, by SDS-PAGE and HPLC

Endotoxin Level

Less than 1 EU/ug of MIF as determined by LAL method.

Predicted Molecular Mass

13.5 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Activity

MIF Protein is fully biologically active when compared to standard. The specific activity is determined by binding rhCD74 in a functional ELISA.

Protein / Peptide Type

Recombinant Protein

Formulation, Preparation, and Storage

NBP2-35005
Formulation Lyophilized from a 0.2 um filtered concentrated solution in PBS, pH 7.4.
Preservative No Preservative
Concentration Lyoph
Reconstitution Recommended to centrifuge prior to opening. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0mg/mL.
Format Carrier-Free
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Store at -20 to -70C as supplied. After reconstitution, store at 2 to 8C for 1 month and at -20 to -70C for long term storage. Avoid repeated freeze-thaw cycles.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: MIF

Migration Inhibitory Factor (MIF) is a secreted protein without a cleavable signal sequence and is secreted via a specialized, nonclassical pathway. It is secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. MIF consists of two alpha-helices and six beta-strands, four of which form a beta-sheet. The two remaining beta-strands interact with other MIF molecules, creating a trimer. Structure-function studies suggest MIF is bifunctional with segregated topology. The N- and C-termini mediate enzyme activity (in theory). Phenylpyruvate tautomerase activity (enol-to-keto) has been demonstrated and is dependent upon Pro at position 1. Amino acids 50-65(a.a.) have also been suggested to contain thiol-protein oxidoreductase activity. MIF has proinflammatory cytokine activity centered around 49 - 65(a.a.). On fibroblasts, MIF induces, IL-1, IL-8 and MMP expression; on macrophages, MIF stimulates NO production and TNF-alpha release folllowing IFN-gamma activation. MIF apparently acts through CD74 and CD44, likely in some form of trimeric interaction. Human MIF is active on mouse cells. Human MIF is 90 %, 94 %, 95 %, and 90 % a.a. identical to mouse, bovine, porcine and rat MIF, respectively.

Long Name

Macrophage Migration Inhibitory Factor

Alternate Names

EC 5.3.2.1, EC 5.3.3.12, GIFmacrophage migration inhibitory factor, GLIF, Glycosylation-inhibiting factor, L-dopachrome isomerase, L-dopachrome tautomerase, macrophage migration inhibitory factor (glycosylation-inhibiting factor), MMIF, Phenylpyruvate tautomerase

Gene Symbol

MIF

Additional MIF Products

Product Documents for Recombinant Human MIF His (C-Term) Protein

Certificate of Analysis

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Product Specific Notices for Recombinant Human MIF His (C-Term) Protein

This product is for research use only and is not approved for use in humans or in clinical diagnosis. This product is guaranteed for 1 year from date of receipt.

Citations for Recombinant Human MIF His (C-Term) Protein

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