Mouse myeloma cell line NS0-derived recombinant human Complement Factor D Ile26-Ala253 Accession # P00746
Specificity
Detects human Complement Factor D in direct ELISAs and Western blots. In direct ELISAs, approximately 10% cross-reactivity with recombinant mouse Complement Factor D is observed, and less than 1% cross-reactivity with recombinant human (rh) Complement Factor B and rhComplement Factor I is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
CFD
Purity Statement
Antigen Affinity-purified
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Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Complement Factor D/Adipsin Antibody [Unconjugated]
Adipsin
ADN
ADNcomplement factor D
AMBP-1
C3 convertase activator
CFD
complement factor D (adipsin)
complement factor D preproprotein
Complement Factor D
D component of complement (adipsin)
DF
EC 3.4.21
EC 3.4.21.46
PFD
Properdin factor DADIPSIN
Background
Complement Factor D 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 (1). It is an exceptionally specific protease and the only known protein substrate is factor B in complex with C3 (2). 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 (3).
White, R.T. et al. (1992) J. Biol. Chem. 267:9210.
Taylor, F.R. et al. (1999) Biochemistry 38:2849.
Kim, S. et al. (1995) J. Biol. Chem. 270:24399.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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