推薦產品
生物源
goat
共軛
alkaline phosphatase conjugate
抗體表格
affinity isolated antibody
抗體產品種類
secondary antibodies
無性繁殖
polyclonal
形狀
buffered aqueous glycerol solution
物種活性
human
技術
direct ELISA: 1:2,000-1:21,000
運輸包裝
wet ice
儲存溫度
2-8°C
目標翻譯後修改
unmodified
一般說明
Immunoglobulins are glycoprotein antibodies that contain two equivalent light chains and a pair of identical heavy chains. Immunoglobulin light chains are the primary protein components of the amyloid fibrillar substance that is present in patients having myeloma-associated amyloidosis . Furthermore, urinary free immunoglobulin light chains can be used for the immunodiagnosis of Bence Jones proteinuria . Anti-Human λ Light Chains (Bound and Free)-Alkaline Phosphatase antibodies are specific for human λ light chains when tested against bound κ and λ proteins (human IgA, IgG, IgM) and free Bence Jones κ and λ myeloma proteins.
Mammalian immunoglobins contain either lambda or kappa light chains.
Alkaline Phosphatase is an enzyme that catalyzes the conversion of chromogenic substrates such as p-nitrophenylphosphate (PNPP); chemiluminescent substrates such as CDP-Star® and fluorogenic substrates such as 4-methylumbelliferyl phosphate (4-MUP) into detectable chromophores, light-emitters or fluorescers, respectively.
Alkaline Phosphatase is an enzyme that catalyzes the conversion of chromogenic substrates such as p-nitrophenylphosphate (PNPP); chemiluminescent substrates such as CDP-Star® and fluorogenic substrates such as 4-methylumbelliferyl phosphate (4-MUP) into detectable chromophores, light-emitters or fluorescers, respectively.
免疫原
λ light chains isolated from Bence Jones urines
應用
Goat polyclonal anti-Human Lambda Light Chains (Bound and Free)-Alkaline Phosphatase antibody may be used to detect human lamba light chain containing immunoglobulins by chromogenic, fluorogenic, and chemiluminescent techniques. Whole cell bacterial ELISAs were performed to detect the light and heavy fragments of monoclonal antibodies against the meningococcal porA protein. The alkaline phosphatase conjugated goat anti-human λ Light Chains IgG was used as the secondary. The reaction was developed using p-nitrophenyl phosphate substrate (Sigma).
外觀
Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2, 50% glycerol and 15 mM sodium azide
法律資訊
CDP-Star is a registered trademark of Tropix, Inc.
免責聲明
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 2
閃點（°F）
Not applicable
閃點（°C）
Not applicable
A Solomon et al.
The Journal of clinical investigation, 70(2), 453-460 (1982-08-01)
An antiserum prepared against a lambda-Bence Jones protein from a patient (SUT) who had multiple myeloma and amyloidosis had specificity for lambda-light chains of the chemically defined variable (V) region lambda-chain subgroup lambda VI. Sequence analyses of protein SUT and
M Weller et al.
Journal of neurology, 239(8), 455-459 (1992-10-01)
Serum IgG and IgM antibodies to gangliosides GM1, GM2, GM3, AGM1, GD1a, GD1b and GT1b were determined in 210 patients with different degenerative and inflammatory disorders including motor neuron diseases, peripheral radiculopathies and neuropathies, multiple sclerosis and neuroborreliosis. No single
Takanari Nakano et al.
Clinical chemistry and laboratory medicine, 42(4), 429-434 (2004-05-19)
The aim of this study was to evaluate the diagnostic efficacy of the ratio of urinary free light chain (FLC) kappa to lambda (kappa/lambda ratio) for the detection of Bence Jones protein (BJP). Urine specimens were collected from 243 patients
Jonas V Schaefer et al.
Protein engineering, design & selection : PEDS, 25(10), 485-506 (2012-07-06)
Recombinant antibodies and their derivatives are receiving ever increasing attention for many applications. Nevertheless, they differ widely in biophysical properties, from stable monomers to metastable aggregation-prone mixtures of oligomers. Previous work from our laboratory presented the combination of structure-based analysis
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