CST is continuously expanding their portfolio to meet your research needs.
Check out some of the latest new products and hot targets, as well as new downloadable resources!
CAR-T Therapy Research Tools: Detect CAR Surface Expression 
Chimeric antigen receptor (CAR) T therapy is a revolutionary type of adoptive cell immunotherapy, which employs genetic engineering to redirect the specificity of cytotoxic T lymphocytes to a tumor antigen(s) expressed on the surface of tumor cells.
Cell Signaling Technology has released products that are ideal for product characterization as well monitoring CAR-T trafficking and persistence. G4S and Whitlow/218 Linker antibodies are available now!
CST offers a diverse array of antibodies against targets in relevant signaling pathways, enabling you to evaluate downstream outcomes and better understand CAR-T cell behavior. Check out the CAR Signaling Network pathway.
VHL (E3X9K) Rabbit mAb -Rabbit-mAb.png)
#81292
E3 ligase is important for cancer and hypoxia signaling
The VHL (Von Hippel-Lindau) protein is a substrate recognition component of an E3
ubiquitin ligase complex containing Elongin BC (TCEB1 and TCEB2), CUL1, and RBX1.
Loss of VHL protein function results in a dominantly inherited familial cancer syndrome
that manifests as angiomas of the retina, hemangioblastomas of the central nervous
system, renal clear cell carcinomas, and pheochromocytomas. Under normoxic
conditions, VHL directs the ubiquitylation and subsequent proteasomal degradation
of the HIF-1α, maintaining very low levels of HIF-1α in the cell. Cellular exposure to
hypoxic conditions, or loss of VHL protein function, results in increased HIF-1α protein
levels and increased expression of HIF-induced gene products, many of which are
angiogenesis factors such as VEGF. Thus, loss of VHL protein function is believed to
contribute to the formation of highly vascular neoplasias.
KEYWORDS: Ubiquitin/Proteasome, Proteolysis, Cancer, Hypoxia signaling
Validated for: IHC
TFEB (E4I8R) Mouse mAb
#91767 
Transcription factor important for lysosome and autophagy
TFEB is a transcription factor of the Myc-related, bHLH leucine-zipper family
member. TFEB specifically recognizes and binds the CLEAR box (GTCACGTGAC)
of lysosomal and autophagy genes, resulting in the upregulated expression of
genes involved in lysosome biogenesis and function, and regulation of autophagy.
TFEB is activated in response to nutrient deprivation, stimulating translocation to
the nucleus where it forms homo- or heterooligomers with other members of the
MiTF subfamily and resulting in upregulation of autophagosomes and lysosomes.
Recently, it has been shown that TFEB is a component of mTORC1, which
regulates the phosphorylation and nuclear translocation of TFEB in response
to cellular starvation and stress. During normal growth conditions, TFEB is
phosphorylated at Ser211 in an mTORC1-dependent manner. Phosphorylation
promotes association of TFEB with 14-3-3 family proteins and retention in the
cytosol. Inhibition of mTORC1 results in a loss of TFEB phosphorylation, dissociation
of the TFEB/14-3-3 complex, and rapid transport of TFEB to the nucleus where it
increases transcription of CLEAR and autophagy genes.
KEYWORDS: Lysosome, Autophagy, Nutrient
Validated for: WB IP IF
p16 INK4A (BC42) Mouse mAb
#68410 
The VHL (Von Hippel-Lindau) protein is a substrate recognition component of an E3
ubiquitin ligase complex containing Elongin BC (TCEB1 and TCEB2), CUL1, and RBX1.
Loss of VHL protein function results in a dominantly inherited familial cancer syndrome
that manifests as angiomas of the retina, hemangioblastomas of the central nervous
system, renal clear cell carcinomas, and pheochromocytomas. Under normoxic
conditions, VHL directs the ubiquitylation and subsequent proteasomal degradation
of the HIF-1α, maintaining very low levels of HIF-1α in the cell. Cellular exposure to
hypoxic conditions, or loss of VHL protein function, results in increased HIF-1α protein
levels and increased expression of HIF-induced gene products, many of which are
angiogenesis factors such as VEGF. Thus, loss of VHL protein function is believed to
contribute to the formation of highly vascular neoplasias.
KEYWORDS: aging, cancer
Validated for: IHC
Phospho-HDAC2 (Ser394) (E8O2Z) Rabbit mAb
#69238 
Acetylation of the histone tail causes chromatin to adopt an “open” conformation,
allowing increased accessibility of transcription factors to DNA. The identification
of histone acetyltransferases (HATs) and their large multiprotein complexes
has yielded important insights into how these enzymes regulate transcription.
HAT complexes interact with sequence-specific activator proteins to target specific
genes. In contrast, histone deacetylation promotes a “closed” chromatin
conformation and typically leads to repression of gene activity. Mammalian
histone deacetylases can be divided into three classes on the basis of their
similarity to various yeast deacetylases. Inhibitors of HDAC activity are now
being explored as potential therapeutic cancer agents.
Picture: C&R: CUT&RUN was performed with K-562 cells and either Phospho-HDAC2 (Ser394) (E8O2Z) Rabbit mAb or Rabbit (DA1E) mAb IgG XP® Isotype Control (CUT&RUN) #66362, using CUT&RUN Assay Kit #86652. The enriched DNA was quantified by real-time PCR using human NBPF1 promoter primers, human DTL exon 1 primers, and human ROBO1 promoter primers. The amount of immunoprecipitated DNA in each sample is represented as signal relative to the total amount of input chromatin, which is equivalent to one.
KEYWORDS: epigenetic regulation, cancer
Validated for: WB IP Flow C&R
Ubiquitin (E6K4Y) XP® Rabbit mAb
#20326
Ubiquitin is a conserved polypeptide unit that plays an important role in
the ubiquitin-proteasome pathway. Ubiquitin can be covalently linked to
many cellular proteins by the ubiquitination process, which targets
proteins for degradation by the 26S proteasome. Three components are
involved in the target protein-ubiquitin conjugation process.
Keywords: targeted protein degradation, DNA damage and repair, cell
cycle progression, apoptosis, receptor-mediated endocytosis, and signal
transduction.
Validated for: WB IHC