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anti-Human TULP1 Antibodies:
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Data suggest that mutant tubby like protein 1 (TULP1) proteins are misfolded and accumulate within the endoplasmic reticulum (ER) leading to induction of the unfolded protein response (UPR) stress response complex.
The TULP1 allele p.Gln301* represents a founder mutation on the Arabian Peninsula and is associated with a recognisable congenital recessive rod-cone dystrophy phenotype in the homozygous state.
Retinal degeneration with TULP1 mutations leads to a small central island of residual foveal cones at early ages which are less sensitive than expected from the residual structure.
Tubby and Tulp1 mediated phagocytosis through MerTK-dependent signaling with non-muscle myosin II redistribution leading to colocalization of phagocytosed vesicles with rearranged NMMIIA.
Maternal uniparental isodisomy of chromosome 6 unmasked a mutation in the TULP1 gene as a novel cause of cone dysfunction.
The single nucleotide polymorphisms rs4374383 and rs9380516 were linked to the functionally related genes MERTK (show MERTK Antibodies) and TULP1, which encode factors involved in phagocytosis of apoptotic cells by macrophages.
One recurrent (c.1138A>G; p.Thr380Ala) and one novel (c.1445G>A; p.Arg482Gln) mutations in TULP1 have been identified in Pakistani families with early-onset retinitis pigmentosa.
Homozygous autosomal recessive retinitis pigmentosa-causing mutations have been found in three Indian families. These included a missense mutation in TULP1.
Pathogenic mutations in TULP1 are responsible for the autosomal recessive retinitis pigmentosa phenotype in these consanguineous Pakistani families, with a single ancestral mutation in TULP1 causing the disease phenotype in 4 of 5 families.
Tubby (show TUB Antibodies) and Tulp1 are bridging molecules with their N-terminal region as MERTK (show MERTK Antibodies)-binding domain and C-terminal region as phagocytosis prey-binding domain.
Tulp1 is essential to keep endocytotic proteins enriched at the periactive zone in photoreceptor ribbon synapses.
Data suggest that photoreceptors-specific protein Tulp1 is involved in the trafficking of proteins from the inner segment (IS) to the outer segment (OS) and the continuous membrane remodeling and vesicle cycling at the synaptic terminal.
Although MAP1A (show MAP1A Antibodies) and MAP1B (show MAP1B Antibodies) protein levels are not affected in the tulp1-/- retina, they are no longer localized to the outer segment of photoreceptors.
Mtap1a (show MAP1A Antibodies), which modifies hearing loss in Tub(tub/tub (show TUB Antibodies)) mice, also modifies retinal degeneration in Tub (show TUB Antibodies) and Tulp1 mice; functionally nonredundant members of the TULP family (TUB (show TUB Antibodies) and TULP1) share a common functional interaction with MTAP1A (show MAP1A Antibodies)
Outer segment proteins are affected differently in Tulp1-/- mice, providing evidence that Tulp1 functions in selective outer segment pathways.
A new mutation in Tulp1 was identifies in a mouse model of retinal degeneration.
These data implicate Tulp1 in the transport of selective integral membrane outer segment proteins and their associated proteins, specifically, the opsin and guanylate cyclase carrier pathways.
Tulp1 is not only critical for photoreceptor function and survival, but is essential for the proper development of the photoreceptor synapse.
Tubby (show TUB Antibodies) and Tulp1 function as phagocytosis sigmals (eat-me) for retinal pigment epithelium cells and other phagocytes.
This gene encodes a member of the tubby-like gene family (TULPs). Members of this family have been identified in plants, vertebrates, and invertebrates and encode proteins of unknown function. TULP proteins share a conserved C-terminal region of approximately 200 amino acid residues. Mutations in this gene may be associated with retinitis pigmentosa.
tubby like protein 1
, tubby-like 1
, tubby-like protein
, tubby-related protein 1-like
, tubby-related protein 1
, tubby like protein 1 like
, tubby-like protein 1