protein

Recombinant human Tumor necrosis factor receptor superfamily member 1A

MBS717308

0.05 mg

195 USD

Recombinant Protein

Recombinant human Tumor necrosis factor receptor superfamily member 1A

Tumor necrosis factor receptor superfamily member 1A

Recombinant human Tumor necrosis factor receptor superfamily member 1A protein

tumor necrosis factor receptor superfamily member 1A; Tumor necrosis factor receptor superfamily member 1A; tumor necrosis factor receptor superfamily member 1A; TNF-R1; TNF-RI; TNFR-I; tumor necrosis factor-alpha receptor; tumor necrosis factor receptor type 1; tumor necrosis factor binding protein 1; tumor necrosis factor receptor 1A isoform beta; tumor necrosis factor receptor superfamily, member 1A; Tumor necrosis factor receptor 1; TNF-R1; Tumor necrosis factor receptor type I; TNF-RI; TNFR-I; p55; p60

TNFRSF1A; TNFRSF1A; FPF; p55; p60; TBP1; TNF-R; TNFAR; TNFR1; p55-R; CD120a; TNFR55; TNFR60; TNF-R-I; TNF-R55; TNFAR; TNFR1; TNF-R1; TNF-RI; TNFR-I; TBPI

TNR1A_HUMAN

E Coli

VPHLGDREKRDSVCPQGKYIHPQNNSICCTKCHKGTYLY
NDCPGPGQDTDCRECESGSFTASENHLRHCLSCSKCRKE
MGQVEISSCTVDRDTVCGCRKNQYRHYWSENLFQCFNCS
LCLNGTVHLSCQEKQNTVCTCHAGFFLRENECVSCSNCK
KSLECTKLCLPQIENVKGTEDSGT

0.9

Store at -20 degree C. For extended storage, conserve at -20 or -80 degree C.

Tag Information: GST tagged

Storage Buffer: PBS pH 7.4, 50% glycerol

Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase.

[1] "Molecular cloning and expression of the human 55 kd tumor necrosis factor receptor.

4507575

NP_001056.1

NM_001065.3

P19438

46 KD

Adipocytokine Signaling Pathway 83093!!Adipocytokine Signaling Pathway 505!!Alzheimer's Disease Pathway 83097!!Alzheimer's Disease Pathway 509!!Amyotrophic Lateral Sclerosis (ALS) Pathway 83099!!Amyotrophic Lateral Sclerosis (ALS) Pathway 511!!Apoptosis Pathway 198797!!Apoptosis Pathway 83060!!Apoptosis Pathway 470!!Apoptosis Pathway 105648

The protein encoded by this gene is a member of the TNF-receptor superfamily. This protein is one of the major receptors for the tumor necrosis factor-alpha. This receptor can activate NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRADD and TRAF2 have been shown to interact with this receptor, and thus play regulatory roles in the signal transduction mediated by the receptor. Germline mutations of the extracellular domains of this receptor were found to be associated with the autosomal dominant periodic fever syndrome. The impaired receptor clearance is thought to be a mechanism of the disease. [provided by RefSeq, Jul 2008]

Function: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Subunit structure: Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BRE, FEM1B, GRB2, SQSTM1 and TRPC4AP. Interacts with HCV core protein. Interacts with human cytomegalovirus/HHV-5 protein UL138. Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19. Subcellular location: Cell membrane; Single-pass type I membrane protein. Secreted. Domain: The domain that induces A-SMASE is probably identical to the death domain. The N-SMASE activation domain (NSD) is both necessary and sufficient for activation of N-SMASE.Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP . By similarity. Post-translational modification: The soluble form is produced from the membrane form by proteolytic processing. Involvement in disease: Defects in TNFRSF1A are the cause of familial hibernian fever (FHF) [. MIM:142680]; also known as tumor necrosis factor receptor-associated periodic syndrome (TRAPS). FHF is a hereditary periodic fever syndrome characterized by recurrent fever, abdominal pain, localized tender skin lesions and myalgia. Reactive amyloidosis is the main complication and occurs in 25% of cases. Ref.22 Ref.23 Ref.24 Ref.25 Ref.26. Sequence similarities: Contains 1 death domain.Contains 4 TNFR-Cys repeats.

0.05 mg

195 USD