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Human BAFF (CD257) Recombinant

BAFF

accession:  Q9Y275
   Size A     5g   $ 70
   Size B      20ug  $160
   Size C      1mg  $ 4700
Domain  :  TNF
Gene  :  TNFSF13B
Catalog no. :  RKQ9Y275
Source:
Optimized DNA sequence encoding Human BAFF extracellular domain was expressed in Escherichia Coli

 
Molecular weight:
Recombinant human BAFF,  is a disulfide-linked monomeric protein consisting of 153 amino acid residue subunits. The molecule has a calculated molecular mass of approximately 18 kDa and migrates as an approximately 18 kDa protein under non-reducing and reducing conditions in SDS-PAGE.

 
Purity:
>95%, as determined by SDS-PAGE and HPLC

 
Biological Activity:
The ED(50) was determined by a cell proliferation assay using anti-IgM stimulated murine B cells, and is less than 2 ng/ml, corresponding to a specific activity of 5.0 × 105 IU/mg

 
Protein Sequence:
        10         20         30         40         50         60 
MDDSTEREQS RLTSCLKKRE EMKLKECVSI LPRKESPSVR SSKDGKLLAA TLLLALLSCC 

        70         80         90        100        110        120 
LTVVSFYQVA ALQGDLASLR AELQGHHAEK LPAGAGAPKA GLEEAPAVTA GLKIFEPPAP 

       130        140        150        160        170        180 
GEGNSSQNSR NKRAVQGPEE TVTQDCLQLI ADSETPTIQK GSYTFVPWLL SFKRGSALEE 

       190        200        210        220        230        240 
KENKILVKET GYFFIYGQVL YTDKTYAMGH LIQRKKVHVF GDELSLVTLF RCIQNMPETL 

       250        260        270        280 
PNNSCYSAGI AKLEEGDELQ LAIPRENAQI SLDGDVTFFG ALKLL 
(*)Complete precursor sequence shown, expressed chain highlighted
 
Endotoxin:
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

 
Presentation:
Recombinant Human BAFF was lyophilized from a 0.2 μm filtered solution in PBS, pH 7.5.

 
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 2 years from date of receipt at -20° 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:
This cytokine product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.

 

BAFF

The B cell-activating factor from the TNF family (BAFF), is emerging as an important regulator of B cell and T cell responses. BAFF was originally identified as a factor responsible for B cell survival and maturation .BAFF binds to several receptors. These include transmembrane activator and calcium modulator and cyclophilin ligand interactor (TACI), BAFF-R (BR3), and B cell maturation Ag (BCMA). BAFF-R appears to be particularly important for the regulation of B cell survival and maturation in the spleen, because A/WySnJ mice expressing a defective BAFF-R have disrupted B cell maturation, similar to that seen in BAFF-deficient mice.

Related Publications:
soluble BAFF levels inversely correlate with peripheral b cell numbers and the expression of BAFF receptors
J. Immunol., Jan 2012; 188: 497 - 503.
BAFF/april inhibition decreases selection of naive but not antigen-induced autoreactive b cells in murine systemic lupus erythematosus
J. Immunol., Dec 2011; 187: 6571 - 6580.
increased levels of BAFF in patients with systemic lupus erythematosus are associated with acute-phase reactants, independent of BAFF genetics: a case–control study
Rheumatology, Dec 2011; 50: 2197 - 2205.
patterns of b cell activating factor (BAFF) levels, b cell recovery, and BAFF/b cell ratios correlate with the development of chronic graft-versus-host disease (cgvhd) following hematopoietic stem cell transplantation (hsct)
Blood (ASH Annual Meeting Abstracts), Nov 2011; 118: 3036.
a lymphoma-associated mutation in BAFF-r drives constitutive pi3k signaling and increased expression of pro-survival genes
Blood (ASH Annual Meeting Abstracts), Nov 2011; 118: 2642.




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