PRS2397
Anti-BCMA antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-Tumor necrosis factor receptor superfamily, member 17
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All Photos(3)
About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
Recommended Products
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
predicted mol wt 20 kDa
species reactivity
human
technique(s)
immunofluorescence: suitable
immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... TNFRSF17(608)
General description
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.
Immunogen
a synthetic peptide mapping at the carboxy-terminus of human BCMA.
Biochem/physiol Actions
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.
Linkage
The action of this antibody can be blocked using blocking peptide SBP2397.
Physical form
Solution in phosphate buffered saline containing 0.02% sodium azide
Disclaimer
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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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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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
Sarah A Laurent et al.
Nature communications, 6, 7333-7333 (2015-06-13)
Survival of plasma cells is regulated by B-cell maturation antigen (BCMA), a membrane-bound receptor activated by its agonist ligands BAFF and APRIL. Here we report that γ-secretase directly cleaves BCMA, without prior truncation by another protease. This direct shedding is
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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