RIPK1 antibody (Receptor (TNFRSF)-Interacting serine-threonine Kinase 1)

Details for Product anti-RIPK1 Antibody No. ABIN967307, Supplier: Log in to see
Antigen
  • C9orf12
  • RGD1311271
  • rIpk1
  • RIP
  • RIP1
  • D330015H01Rik
  • Rinp
  • Rip1
  • 2400006N03Rik
  • RP23-83I13.5
  • Rip
  • receptor (TNFRSF)-interacting serine-threonine kinase 1
  • inositol 1,3,4,5,6-pentakisphosphate 2-kinase
  • RPA interacting protein
  • LOC100230522
  • Ippk
  • RIPK1
  • Ripk1
  • Rpain
Alternatives
anti-Human RIPK1 antibody for Immunohistochemistry (Frozen Sections)
Reactivity
Human
136
40
40
11
4
4
3
2
1
1
Host
Mouse
99
34
3
Clonality (Clone)
Monoclonal ()
Conjugate
This RIPK1 antibody is un-conjugated
4
4
3
3
2
2
2
2
2
1
1
1
1
1
1
1
1
Application
Immunoprecipitation (IP), Western Blotting (WB)
110
45
40
32
28
16
9
4
3
2
2
Options
Supplier
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Supplier Product No.
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Brand BD Pharmingen™
Immunogen truncated RIP fusion protein
Clone G322-2
Isotype IgG1, kappa
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name RIP (RIPK1 Antibody Abstract)
Background RIP (receptor interacting protein) is a 74 kDa serine/threonine kinase which may be recruited to TNFR type 1 and Fas (CD95) receptor signal complexes following ligand binding. RIP interacts with other signal proteins within these complexes (e.g., RAIDD) and has also been shown to interact with pro-caspase-2. RIP contains an N-terminal kinase domain as well as a C-terminal death domain that is homologous to intracellular death domain of Fas. Over expression of RIP in vitro is sufficient to induce cell death, demonstrating that RIP functions as an apoptosis-inducing protein. Interaction of the Fas death domain with other intracellular proteins like RIP is an important step leading to downstream components in apoptotic signaling pathways. Clone G322-2 recognizes human RIP. A recombinant truncated human RIP:tagged fusion protein, lacking the kinase domain of RIP, was used as immunogen. The specificity of the antibody was verified by ELISA, immunoprecipitation and western blot analysis. The antibody is routinely tested by western blot analysis in human Jurkat T cells where it recognizes RIP as a 74 kDa band. Smaller molecular weight breakdown bands of ~30 kDa, 22 kDa, and/or 16 kDa are sometimes observed.
Molecular Weight 74 kDa
Research Area Cancer, Apoptosis/Necrosis
Pathways NF-kappaB Signaling, Apoptosis, Caspase Cascade in Apoptosis, TLR Signaling, Activation of Innate immune Response, Inositol Metabolic Process, Positive Regulation of Endopeptidase Activity, Hepatitis C, Protein targeting to Nucleus, Toll-Like Receptors Cascades, Negative Regulation of intrinsic apoptotic Signaling
Application Notes Additional control lysate (ABIN968537) is sold separately.
Comment

Related Products: ABIN968537

Restrictions For Research Use only
Format Liquid
Concentration 0.25 mg/mL
Buffer Aqueous buffered solution containing BSA, glycerol, and ≤0.09 % sodium azide.
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Storage Comment Store undiluted at -20°C.
Supplier Images
Western Blotting (WB) image for anti-Receptor (TNFRSF)-Interacting serine-threonine Kinase 1 (RIPK1) antibody (ABIN967307) Western blot analysis of RIP. Lysate from Jurkat cells was probed with anti-RIP (clon...
Product cited in: Stanger, Leder, Lee, Kim, Seed: "RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death." in: Cell, Vol. 81, Issue 4, pp. 513-23, 1995 (PubMed).

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