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product-image-AAA161865_BIOACTIVITY13.jpg Bioactivity (Complement Factor D (CFD) is a serine protease that catalyzes the initial proteolytic step in the alternative pathway of complement. Expressed in adipose tissue at high levels, factor D is also known as adipsin. It is an exceptionally specific protease and the only known protein substrate is factor B in complex with C3. Factor D protease activity is regulated by reversible conformational changes, which differs from the majority of serine proteases whose regulation involves either activation by processing of the zymogens or inactivation by binding of the inhibitors. Compared to its physiologically important proteolytic activity, factor D has much lower activity toward synthetic peptide substrates. However, thioester substrates have been routinely used for assessing factor D activity. The full-length (amino acid residues 1-263) of rat CFD was expressed which activity was measured by its ability to cleaves a thioester substrate Z-Lys-SBzl•HCl. The reaction was performed in 50 mM Tris, 1 M NaCl, pH 7.5 (Assay Buffer), initiated by addition 50 uL of various concentrations of CFD (diluted by Assay Buffer) to 50 ul substrate mixture of 0.2mM Z-Lys-SBzl•HCl and 0.2 mM DTNB. The final well serves as a negative control with no CFD, replaced with 50 ul assay buffer. Then read in kinetic mode for 5 minutes at an absorbance of 405 nm. The specific activity of recombinant rat CFD is > 10000 pmol/min/ug.)

Complement Factor D (CFD) Active Protein | CFD active protein

Active Complement Factor D (CFD)

Gene Names
Cfd; Df; Adn; EVE
Applications
Activity Assay, Cell Culture
Purity
Greater than 95% by SDS-PAGE
Synonyms
Complement Factor D (CFD); N/A; Active Complement Factor D (CFD); Complement Factor D; CF-D; DF; PFD; ADN; Adipsin; Properdin Factor D; C3 convertase activator4; CFD active protein
Ordering
Host
E Coli
Purity/Purification
Greater than 95% by SDS-PAGE
Form/Format
Freeze-dried powder; PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
Sequence
Met1~Ala263
Applicable Applications for CFD active protein
Activity Assay, Cell Culture
Species
Rat
Expression System
Prokaryotic expression
Tag
N-terminal His Tag
Endotoxin Level
<1.0EU per 1ug (determined by the LAL method)
Isoelectric Point
6.6
Research Area
Immune molecule
Preparation and Storage
Store at 2-8 degree C for one month, -80 degree C for 12 months

Bioactivity

(Complement Factor D (CFD) is a serine protease that catalyzes the initial proteolytic step in the alternative pathway of complement. Expressed in adipose tissue at high levels, factor D is also known as adipsin. It is an exceptionally specific protease and the only known protein substrate is factor B in complex with C3. Factor D protease activity is regulated by reversible conformational changes, which differs from the majority of serine proteases whose regulation involves either activation by processing of the zymogens or inactivation by binding of the inhibitors. Compared to its physiologically important proteolytic activity, factor D has much lower activity toward synthetic peptide substrates. However, thioester substrates have been routinely used for assessing factor D activity. The full-length (amino acid residues 1-263) of rat CFD was expressed which activity was measured by its ability to cleaves a thioester substrate Z-Lys-SBzl•HCl. The reaction was performed in 50 mM Tris, 1 M NaCl, pH 7.5 (Assay Buffer), initiated by addition 50 uL of various concentrations of CFD (diluted by Assay Buffer) to 50 ul substrate mixture of 0.2mM Z-Lys-SBzl•HCl and 0.2 mM DTNB. The final well serves as a negative control with no CFD, replaced with 50 ul assay buffer. Then read in kinetic mode for 5 minutes at an absorbance of 405 nm. The specific activity of recombinant rat CFD is > 10000 pmol/min/ug.)

product-image-AAA161865_BIOACTIVITY13.jpg Bioactivity (Complement Factor D (CFD) is a serine protease that catalyzes the initial proteolytic step in the alternative pathway of complement. Expressed in adipose tissue at high levels, factor D is also known as adipsin. It is an exceptionally specific protease and the only known protein substrate is factor B in complex with C3. Factor D protease activity is regulated by reversible conformational changes, which differs from the majority of serine proteases whose regulation involves either activation by processing of the zymogens or inactivation by binding of the inhibitors. Compared to its physiologically important proteolytic activity, factor D has much lower activity toward synthetic peptide substrates. However, thioester substrates have been routinely used for assessing factor D activity. The full-length (amino acid residues 1-263) of rat CFD was expressed which activity was measured by its ability to cleaves a thioester substrate Z-Lys-SBzl•HCl. The reaction was performed in 50 mM Tris, 1 M NaCl, pH 7.5 (Assay Buffer), initiated by addition 50 uL of various concentrations of CFD (diluted by Assay Buffer) to 50 ul substrate mixture of 0.2mM Z-Lys-SBzl•HCl and 0.2 mM DTNB. The final well serves as a negative control with no CFD, replaced with 50 ul assay buffer. Then read in kinetic mode for 5 minutes at an absorbance of 405 nm. The specific activity of recombinant rat CFD is > 10000 pmol/min/ug.)

SDS-PAGE

(Figure. SDS-PAGE)

product-image-AAA161865_SDS_PAGE15.jpg SDS-PAGE (Figure. SDS-PAGE)
Product Categories/Family for CFD active protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
28,442 Da
NCBI Official Full Name
complement factor D
NCBI Official Synonym Full Names
complement factor D
NCBI Official Symbol
Cfd
NCBI Official Synonym Symbols
Df; Adn; EVE
NCBI Protein Information
complement factor D
UniProt Protein Name
Complement factor D
UniProt Gene Name
Cfd
UniProt Synonym Gene Names
Adn; Df

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Product Notes

The CFD cfd (Catalog #AAA161865) is an Active Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. AAA Biotech's Complement Factor D (CFD) can be used in a range of immunoassay formats including, but not limited to, Activity Assay, Cell Culture. Researchers should empirically determine the suitability of the CFD cfd for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. The amino acid sequence is listed below: Met1~Ala26 3. It is sometimes possible for the material contained within the vial of "Complement Factor D (CFD), Active Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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