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Key Documents

PRS2397

Sigma-Aldrich

Anti-BCMA antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-Tumor necrosis factor receptor superfamily, member 17

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About This Item

Código UNSPSC:
12352203
NACRES:
NA.41

origen biológico

rabbit

conjugado

unconjugated

forma del anticuerpo

affinity isolated antibody

tipo de anticuerpo

primary antibodies

clon

polyclonal

formulario

buffered aqueous solution

mol peso

predicted mol wt 20 kDa

reactividad de especies

human

técnicas

immunofluorescence: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

modificación del objetivo postraduccional

unmodified

Información sobre el gen

human ... TNFRSF17(608)

Descripción general

B-cell maturation antigen (BCMA), commonly known as TNFRSF17 (tumor necrosis factor receptor superfamily member 17), is an N-glycosylated membrane glycoprotein. It is predominantly expressed on the surface of plasma cells, and is also expressed on certain cancers such as, glioblastoma, chronic lymphocytic leukemia, Hodgkin′s lymphoma and multiple myeloma.

Inmunógeno

a synthetic peptide mapping at the carboxy-terminus of human BCMA.

Acciones bioquímicas o fisiológicas

TNFRSF17 (tumor necrosis factor receptor superfamily member 17) is essential for the maintenance of the survival of long-lived plasma cells in bone marrow. Its expression in peripheral blood B-cells is induced by cytokines. It gets activated by a proliferation-inducing ligand (APRIL) or B-cell–activating factor (BAFF), and gets trimerized to activate MAPK (mitogen activated kinases) and anti-apoptotic proteins. It is an appropriate target for T-cells expressing chimeric antigen receptor (CAR), and is a promising candidate for adoptive T-cell therapy of multiple myeloma. This protein is directly cleaved and shed by γ-secretase enzyme, and this is linked with level of plasma cells in bone marrow. Thus, shedding of TNFRSF17 is a candidate biomarker for B-cell involvement in autoimmune diseases. This protein is thought to be a major contributor of spinal cord-injury induced autoimmunity.

Ligadura / enlace

The action of this antibody can be blocked using blocking peptide SBP2397.

Forma física

Solution in phosphate buffered saline containing 0.02% sodium azide

Cláusula de descargo de responsabilidad

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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Código de clase de almacenamiento

10 - Combustible liquids

Clase de riesgo para el agua (WGK)

WGK 2

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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Jonah W Saltzman et al.
Journal of neurotrauma, 30(6), 434-440 (2012-10-24)
Autoimmunity is thought to contribute to poor neurological outcomes after spinal cord injury (SCI). There are few mechanism-based therapies, however, designed to reduce tissue damage and neurotoxicity after SCI because the molecular and cellular bases for SCI-induced autoimmunity are not
Robert O Carpenter et al.
Clinical cancer research : an official journal of the American Association for Cancer Research, 19(8), 2048-2060 (2013-01-25)
Multiple myeloma is a usually incurable malignancy of plasma cells. New therapies are urgently needed for multiple myeloma. Adoptive transfer of chimeric antigen receptor (CAR)-expressing T cells is a promising new therapy for hematologic malignancies, but an ideal target antigen
Han-Wen Huang et al.
Proceedings of the National Academy of Sciences of the United States of America, 110(27), 10928-10933 (2013-06-19)
Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown. In this study, we identified a panel of glycoproteins by click reaction with alkynyl

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