추천 제품
생물학적 소스
goat
Quality Level
결합
alkaline phosphatase conjugate
항체 형태
affinity isolated antibody
항체 생산 유형
secondary antibodies
클론
polyclonal
형태
buffered aqueous glycerol solution
종 반응성
human
기술
direct ELISA: 1:2,000-1:21,000
배송 상태
wet ice
저장 온도
2-8°C
타겟 번역 후 변형
unmodified
일반 설명
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.
면역원
λ light chains isolated from Bence Jones urines
애플리케이션
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).
물리적 형태
Solution in 0.05 M Tris, pH 8.0, containing 1% bovine serum albumin, 1 mM MgCl2, 50% glycerol and 15 mM sodium azide
법적 정보
CDP-Star is a registered trademark of Tropix, Inc.
면책조항
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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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
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
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
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
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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