SAB4500430
Anti-CPB2 antibody produced in rabbit
affinity isolated antibody
别名:
CBPB2, CPU, carboxypeptidase B2, carboxypeptidase U, plasma carboxypeptidase B
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关于此项目
NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA, WB
Citations:
2
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 48 kDa
species reactivity
human
concentration
~1 mg/mL
technique(s)
ELISA: 1:40000, western blot: 1:500-1:1000
NCBI accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CBPB2(1361)
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General description
Anti-CPB2 Antibody detects endogenous levels of total CPB2 protein.
Immunogen
The antiserum was produced against synthesized peptide derived from human CPB2.
Immunogen Range: 321-370
Immunogen Range: 321-370
Application
Anti-CPB2, C-Terminal antibody produced in rabbit is suitable for indirect ELISA and western blot analysis.
Biochem/physiol Actions
CPB2 exhibit antifibrinolytic property. It cleaves the C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins to regulate their activities. By the carboxypeptidase activity, CPB2 release C-terminal Lys and Arg residues from partially degraded fibrin which finally indicates towards an antifibrinolytic effect.
Features and Benefits
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Physical form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
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存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
常规特殊物品
此项目有
S S Mao et al.
The Journal of biological chemistry, 274(49), 35046-35052 (1999-11-27)
Plasma carboxypeptidase B (PCB) is an exopeptidase that exerts an antifibrinolytic effect by releasing C-terminal Lys and Arg residues from partially degraded fibrin. PCB is produced in plasma via limited proteolysis of the zymogen, pro-PCB. In this report, we show
D L Eaton et al.
The Journal of biological chemistry, 266(32), 21833-21838 (1991-11-15)
A novel plasminogen-binding protein has been isolated from human plasma utilizing plasminogen-Sepharose affinity chromatography. This protein copurified with alpha 2 antiplasmin when the plasminogen affinity column was eluted with high concentrations of epsilon-aminocaproic acid (greater than 20 mM). Analysis by
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