Összes fotó(2)
Fontos dokumentumok
A2904
Anti-Human Lambda Light Chains (Bound and Free)−Alkaline Phosphatase antibody produced in goat
affinity isolated antibody, buffered aqueous glycerol solution
Szinonimák:
Goat Anti-Human Lambda Light Chains (Bound and Free)−AP
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(2)
About This Item
Javasolt termékek
biológiai forrás
goat
Minőségi szint
konjugátum
alkaline phosphatase conjugate
antitest forma
affinity isolated antibody
antitest terméktípus
secondary antibodies
klón
polyclonal
Forma
buffered aqueous glycerol solution
faj reaktivitás
human
technika/technikák
direct ELISA: 1:2,000-1:21,000
kiszállítva
wet ice
tárolási hőmérséklet
2-8°C
célzott transzláció utáni módosítás
unmodified
Általános leírás
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.
Immunogén
λ light chains isolated from Bence Jones urines
Alkalmazás
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).
Fizikai forma
Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2, 50% glycerol and 15 mM sodium azide
Jogi információk
CDP-Star is a registered trademark of Tropix, Inc.
Jogi nyilatkozat
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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Tárolási osztály kódja
10 - Combustible liquids
WGK
WGK 2
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
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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
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
J Wang et al.
Infection and immunity, 68(4), 1871-1878 (2000-03-18)
The meningococcal PorA protein is considered a promising vaccine candidate. Although much is understood regarding the structure of PorA proteins, little is known about the structure-function relationships of PorA antibodies. The aim of this study was to compare the functional
D Wang et al.
Leukemia, 31(10), 2114-2121 (2017-02-25)
Multiple myeloma (MM) is a plasma cell malignancy where MM cell growth is supported by the bone marrow (BM) microenvironment with poorly defined cellular and molecular mechanisms. MM cells express CD40, a receptor known to activate autocrine secretion of cytokines
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