Browse our anti-Agouti Signaling Protein (ASIP) Antibodies

Human Agouti Signaling Protein (ASIP) interaction partners

1. ASIP expression is significantly downregulated in human masticatory mucosa during wound healing

2. Polymorphisms of ASIP were found to be associated with skin, hair, and eye color in a phenotypically diverse Brazilian population. More research is needed to determine its usefulness in forensic science.

3. ASIP gene mutation is involved in the development of facial pigmented lesions.

4. Data show that ASIP TG/TG diplotype, which is known to be associated with melanoma risk, was linked to a 5-fold increase in hazard of death from melanoma.

5. An increased risk of melanoma (odds ratio [OR] 1.27, 95% confidence interval [95% CI] 1.03-1.57) in carriers of the rs4911414 variant, located 120 kb upstream of ASIP.

6. By using a population-based material of high-risk melanoma cases, we demonstrate a significant effect of both MC1R red hair color (RHC) variants and an ASIP haplotype, but could not replicate an association with postulated risk SNPs of TYR and TYRP1.

7. Findings suggest that ASIP locus is associated with a number of non-melanoma skin cancers.

8. Further analysis of binding and functional data suggests that the ASIP C-terminal loop (a six-amino-acid segment closed by the final disulfide bond) is essential for high-affinity MC1R binding and inverse agonism.

9. polymorphism in the agouti signaling protein gene is associated with human pigmentation

10. results show that men and women of similar age and BMI present similar agouti signal protein mRNA levels in omental and subcutaneous abdominal adipocytes but a sexual dimorphism exists in the relationship between its expression and BMI

11. Results identify five genes that are down-regulated by agouti signalling protein (ASIP), indicating a likely role for ASIP in human melanogenesis.

12. Agouti mRNA levels significantly elevated in type 2 diabetes. Insulin did not regulate agouti mRNA. Agouti can regulate adipogenesis.There are functional consequences of elevated agouti levels in human adipose tissue.

13. Our study suggests that the ASIP G>A polymorphism exhibits a dominant effect leading to lighter skin color and that variation in the ASIP gene may have been one of several factors contributing to reductions in pigmentation in some populations.

14. ASIP polymorphism was not associated with pigmentation, nevi, or melanoma risk

15. An important role for exon 17b of ASIP in cancer cells was identified;alternative splicing isoforms ,hASIP-sa, hASIP-sb, had different effects on cell growth and Fas/FasL-mediated apoptosis in BEL-7404 human hepatoma cells.

16. A/G polymorphism in the 3'-UTR region of the agouti signaling protein contributes to dark pigmentation.

17. Cocaine- and amphetamine-regulated transcript protein is colocalized with this protein and neuropeptide Y in human hypothalamus.

18. ASIP and TYR pigmentation variants associate with cutaneous melanoma and basal cell carcinoma.

19. Two coding variants in TPCN2 are associated with hair color, and a variant at the ASIP locus shows strong association with skin sensitivity to sun, freckling and red hair.

20. ASIP polymorphism was found not to be associated with skin malignant melanoma or basal cell carcinoma.

Cow (Bovine) Agouti Signaling Protein (ASIP) interaction partners

1. Our results provide evidence for a widespread expression of ASIP in bovine tissues at mRNA and, for the first time, at protein level.

2. Possible consequences of Abr (agouti gene mutated by insertion of LINE element)for meat and milk production in cattle.

Pig (Porcine) Agouti Signaling Protein (ASIP) interaction partners

1. Mutational analysis of the ASIP loci in relation to coat color.

Mouse (Murine) Agouti Signaling Protein (ASIP) interaction partners

1. Loss of endothelial PAR-3 disrupts regional axial cell polarity and increases pro-inflammatory response of endothelial cells.

2. mammary morphogenesis is dependent on the ability of Par3 to directly bind aPKC

3. The structure of par3-PDZ3 peptide bound to the C-terminal tail of vascular endothelial cadherin clearly shows that both canonical and distal interactions are utilized in binding and suggests a mechanism for ligand specificity within the polarity network.

4. results suggest that ERK2 phosphorylates Par3 and inhibits its binding with KIF3A, thereby controlling Par3 transport and neuronal polarity

5. Polycystin-1 binds Par3/PKCalpha and controls convergent extension during renal tubular morphogenesis.

6. Rassf5 and Ndr1 or Ndr2 kinases regulate neuronal polarity through Par3 phosphorylation.

7. support for the hitherto untested model that Par3-mInsc and Galphai3 act cooperatively to polarize LGN and promote perpendicular divisions

8. this study demonstrates a mechanism by which loss of Par3 promotes proliferation and tumorigenesis, which supports a tumor-suppressive function for Par3 in the mammary epithelium.

9. Loss of PAR3 triggers increased production of interleukin-6, which induces STAT3 signaling in an autocrine manner.

10. Par3 is the long-sought exocyst receptor required for targeted membrane-protein delivery.

11. Epidermal aPKClambda and Par3 promote a tumor-permissive environment.

12. Loss of Par3 promotes prostatic tumorigenesis by enhancing cell growth and changing cell division modes

13. radial glial progenitor behavior and cortical development are controlled by temporally distinct actions of partitioning-defective 3 (PARD3) in concert with dynamic HIPPO signaling

14. Par3A function is either dispensable for slit diaphragm integrity, or compensatory mechanisms and a high redundancy of the different polarity proteins

15. Par-3 plays an important role in the modulation of intestinal barrier function by regulating delivery of occludin as well as suppression of MLC phosphorylation.

16. HTT is required for the apical localization of PAR3-aPKC during epithelial morphogenesis in virgin, pregnant, and lactating mice.

17. Authors identify the cell polarity protein Par3, a negative regulator of neuronal differentiation, as a Smek1 substrate and demonstrate that Smek1 suppresses its activity.

18. Par3 (and protein kinase C zeta) are activated in neurons when binding to N2-proteoglygan.

19. Suggest that loss of Par3 promotes metastatic behaviour of ErbB2-induced breast tumour epithelial cells by decreasing cell-cell cohesion.

20. Par3 is identified as a regulator of signaling pathways relevant to invasive breast cancer.

Horse (Equine) Agouti Signaling Protein (ASIP) interaction partners

1. variation in MC1R, ASIP, and MATP genes in horse coat color

2. there was a correlation between the recessive ASIP allele and a more independent temperament