FLIP Antibody | Affinity Biosciences

WB
IHC
Cites

1/4

Western blot analysis of extracts from P19 cells, using CFLAR Antibody.

DF7010 at 1/100 staining Human kidney cancer and adjacent normal tissues by IHC-P.

DF7010 at 1/100 staining Rat brain tissue by IHC-P.

Figure 5.

Product:	FLIP Antibody
Catalog:	DF7010
Description:	Rabbit polyclonal antibody to FLIP
Application:	WB IHC IF/ICC
Reactivity:	Human, Mouse, Rat
Mol.Wt.:	52kDa; 55kD(Calculated).
Uniprot:	O15519
RRID:	AB_2838966

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Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific.

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100ul	$280	In stock
200ul	$350	In stock

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MS Report

HPLC Report

MSDS

Data Sheet

COA

Protocols

WB Handbook

IHC Protocol

IF/ICC Protocol

Product Info

Source:

Rabbit

Application:

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:

Human,Mouse,Rat

Clonality:

Polyclonal

Specificity:

FLIP Antibody detects endogenous levels of total FLIP.

RRID:

AB_2838966
Cite Format: Affinity Biosciences Cat# DF7010, RRID:AB_2838966.

Conjugate:

Unconjugated.

Purification:

The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).

Storage:

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.

Alias:

Fold/Unfold

c FLIP; c FLIPL; c FLIPR; c FLIPS; c-FLIP; c-FLIPL; c-FLIPR; c-FLIPS; CASH; CASP8 and FADD like apoptosis regulator; CASP8 and FADD-like apoptosis regulator subunit p12; CASP8AP1; Caspase homolog; Caspase like apoptosis regulatory protein; Caspase related inducer of apoptosis; Caspase-eight-related protein; Caspase-like apoptosis regulatory protein; Casper; Cellular FLICE-like inhibitory protein; CFLA; Cflar; CFLAR_HUMAN; CLARP; FADD like anti apoptotic molecule; FADD-like antiapoptotic molecule 1; FLAME; FLAME-1; FLAME1; FLIP; I FLICE; I-FLICE; Inhibitor of FLICE; MACH-related inducer of toxicity; MRIT; OTTHUMP00000163715; OTTHUMP00000206475; OTTHUMP00000206476; OTTHUMP00000206478; OTTHUMP00000206479; OTTHUMP00000206480; OTTHUMP00000206482; OTTHUMP00000207360; Usurpin; Usurpin beta;

Immunogens

Immunogen:

Uniprot:

O15519(CFLAR_HUMAN) >>Visit HPA database.

Gene(ID):

CFLAR(8837)

Expression:

O15519 CFLAR_HUMAN:

Widely expressed. Higher expression in skeletal muscle, pancreas, heart, kidney, placenta, and peripheral blood leukocytes. Also detected in diverse cell lines. Isoform 8 is predominantly expressed in testis and skeletal muscle.

Description:

Cellular FLIP (FLICE inhibitory protein) is a regulator of apoptosis that has various names, such as c-FLIP (1), Casper (2), CLARP (3), FLAME (4), I-FLICE (5), MRIT (6), CASH (7), and Usurpin (8). FLIP is expressed as two alternative splice isoforms, FLIP short (FLIPS) and FLIP long (FLIPL). FLIPS contains two death effector domains (DEDs) like those found on the death receptor adaptor protein FADD and the pro-domain of caspase-8. FLIPL shares significant homology with caspase-8 (FLICE), and contains an additional death effector domain, but FLIPL lacks the catalytic active site of the caspases and does not have protease activity. Both FLIP isoforms have been reported to interact with FADD and pro-caspase-8. The role of FLIP in apoptosis is controversial as some research studies have reported it to be anti-apoptotic, while others claim that it is pro-apoptotic. Overexpression of FLIPL can lead to caspase-8 heterodimers that produce an active protease, resulting in apoptosis. However, at physiological levels, it is thought that the binding of FLIP to the DED of FADD results in inhibition of caspase-8 processing. Reduction of FLIP by siRNA or gene targeting sensitizes cells to death receptor-mediated apoptosis. FLIP has also been implicated in the resistance of cancer cells to apoptosis and is upregulated in some cancer types including Hodgkin's lymphoma and ovarian and colon carcinomas (9).

Sequence:

O15519 CFLAR_HUMAN:
Protein BLAST With
NCBI/
ExPASy/
Uniprot

MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVETHLLRNPHLVSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYKQSVQGAGTSYRNVLQAAIQKSLKDPSNNFRLHNGRSKEQRLKEQLGAQQEPVKKSIQESEAFLPQSIPEERYKMKSKPLGICLIIDCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVSRGGSQSVYGVDQTHSGLPLHHIRRMFMGDSCPYLAGKPKMFFIQNYVVSEGQLEDSSLLEVDGPAMKNVEFKAQKRGLCTVHREADFFWSLCTADMSLLEQSHSSPSLYLQCLSQKLRQERKRPLLDLHIELNGYMYDWNSRVSAKEKYYVWLQHTLRKKLILSYT

PTMs - O15519 As Substrate

O15519

Site	PTM Type	Enzyme	Source
K49	Ubiquitination		Uniprot
K77	Ubiquitination		Uniprot
R122	Methylation		Uniprot
K154	Ubiquitination		Uniprot
K157	Ubiquitination		Uniprot
T166	Phosphorylation		Uniprot
K167	Ubiquitination		Uniprot
Y171	Phosphorylation		Uniprot
K172	Ubiquitination		Uniprot
Y182	Phosphorylation		Uniprot
K192	Ubiquitination		Uniprot
S193	Phosphorylation	P17252 (PRKCA) , P05771 (PRKCB)	Uniprot
K195	Ubiquitination		Uniprot
K214	Ubiquitination		Uniprot
K225	Ubiquitination		Uniprot
K226	Ubiquitination		Uniprot
S227	Phosphorylation		Uniprot
S231	Phosphorylation		Uniprot
C254	S-Nitrosylation		Uniprot
C259	S-Nitrosylation		Uniprot
S273	Phosphorylation	P31749 (AKT1)	Uniprot
S314	Phosphorylation		Uniprot
K386	Ubiquitination		Uniprot

Research Backgrounds

O15519_CFLAR_HUMAN

Function:

Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity.

PTMs:

Proteolytically processed by CASP8 generating subunit p43 and p12.

Tissue Specificity:

Subunit Structure:

TNFRSF6 stimulation triggers recruitment to the death-inducing signaling complex (DISC) formed by TNFRSF6, FADD and CASP8. A proteolytic fragment (p43) stays associated with the DISC. Also interacts with FADD, CASP8, CASP3, TRAF1, TRAF2 and Bcl-X(L) (in vitro). Interacts with RIPK1 (By similarity).

(Microbial infection) Interacts with HBV protein X.

Family&Domains:

The caspase domain lacks the active site residues involved in catalysis.

Belongs to the peptidase C14A family.

Research Fields

· Cellular Processes > Transport and catabolism > Autophagy - animal. (View pathway)

· Cellular Processes > Cell growth and death > Apoptosis. (View pathway)

· Cellular Processes > Cell growth and death > Necroptosis. (View pathway)

· Environmental Information Processing > Signal transduction > NF-kappa B signaling pathway. (View pathway)

· Environmental Information Processing > Signal transduction > TNF signaling pathway. (View pathway)

· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).

References

1). Nuclear respiratory factor 1 protects H9C2 cells against hypoxia‐induced apoptosis via the death receptor pathway and mitochondrial pathway. CELL BIOLOGY INTERNATIONAL, 2021 (PubMed: 33913583) [IF=3.9]

Application: WB Species: Mouse Sample: H9C2 cells

Figure 5. Effects of nuclear respiratory factor 1 (NRF-1) on the expression of death reporter pathway-associated genes and proteins in hypoxia-induced H9C2 cells A. The mRNA expression of NRF-1, Fas, FasL, FADD, Cflar, Caspase-8 and Bid were detected by RT-qPCR. β-actin was used as the internal control; B. The protein expression of NRF-1, Fas, FasL, FADD, Cflar, Caspase-8 and Bid was detected by western blot analysis. β-actin was used as the internal control. Band intensity ratios for each group are presented as the mean ± standard deviation (n=3). *p < 0.05 and **p < 0.01; NS, not significant.

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FLIP Antibody - #DF7010