ADP-Ribosylation Factor-Like 13B Proteins (ARL13B)

ARL13B encodes a member of the ADP-ribosylation factor-like family. Additionally we are shipping ARL13B Antibodies (27) and ARL13B Kits (2) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
Rat ARL13B ARL13B 304037  
ARL13B 200894 Q3SXY8
ARL13B 68146 Q640N2
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Top ARL13B Proteins at antibodies-online.com

Showing 5 out of 6 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
Insect Cells Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 60 Days
$7,759.50
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Insect Cells Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 60 Days
$7,759.50
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HOST_Wheat germ Human GST tag 10 μg Log in to see 11 to 12 Days
$405.71
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HOST_HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Log in to see 10 to 12 Days
$785.40
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Yeast Zebrafish His tag   1 mg Log in to see 60 to 71 Days
$3,129.50
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ARL13B Proteins by Origin and Source

Origin Expressed in Conjugate
Human , ,
, ,
Mouse (Murine)

More Proteins for ADP-Ribosylation Factor-Like 13B (ARL13B) Interaction Partners

Zebrafish ADP-Ribosylation Factor-Like 13B (ARL13B) interaction partners

  1. loss of Arl13b leads to slow photoreceptor degeneration, but can be exacerbated by the loss of vangl2 (show VANGL2 Proteins). Importantly, the data show that Arl13b can genetically and physically interact with Vangl2 (show VANGL2 Proteins) and this association is important for normal photoreceptor structure.

  2. Arl13b is an important effector of ciliary membrane biogenesis and ciliary length regulation.

  3. Cilia localization is essential for in vivo functions of the Joubert syndrome protein arl13b.

Human ADP-Ribosylation Factor-Like 13B (ARL13B) interaction partners

  1. Our results show how Arl13b participates in Hedgehog (show SHH Proteins) pathway activation in gastric cancer

  2. Reduced primary cilia length and altered Arl13b expression are associated with deregulated chondrocyte Hedgehog (show SHH Proteins) signaling in alkaptonuria (show HGD Proteins).

  3. ARL13B regulates IFT-A-mediated retrograde protein trafficking within cilia through its interaction with INPP5E.

  4. Biochemical characterization of purified mammalian ARL13B protein indicates that it is an atypical GTPase (show RACGAP1 Proteins) and ARL3 guanine nucleotide exchange factor (show RASGRF1 Proteins) (GEF (show SLC2A4RG Proteins)).(

  5. Thus our data identify a novel ARL13B variant that causes JS and retinopathy and suggest an extension of the phenotypic spectrum of ARL13B mutations to obesity.

  6. We conclude that MKS/NPHP modules comprise a TZ barrier to ARL-13 diffusion, whereas IFT genes predominantly facilitate ARL-13 ciliary entry and/or retention via active transport mechanisms.

  7. X-ray crystallography of Arl13B demonstrates involvement of mutations R79Q and R200C in stabilizing intramolecular interactions.

  8. Arl13b acts as the all-rounder in cilia formation and signaling (Review).

  9. findings indicate that ARL13B, INPP5E, PDE6D (show PDE6D Proteins), and CEP164 form a distinct functional network that is involved in JBTS and NPHP but independent of the ones previously defined by NPHP and MKS (show MKS1 Proteins) proteins

  10. data reveal a novel but conserved role for the SUMOylation modification of ciliary small GTPase (show RACGAP1 Proteins) ARL13B in specifically regulating the proper ciliary targeting of various sensory receptors

Mouse (Murine) ADP-Ribosylation Factor-Like 13B (ARL13B) interaction partners

  1. Arl13b dysfunction resulted in hennin cell stagnation due to poor growth factor signaling and impaired detection of extracellular electrical gradients.

  2. Biochemical characterization of purified mammalian ARL13B protein indicates that it is an atypical GTPase (show RACGAP1 Proteins) and ARL3 guanine nucleotide exchange factor (show ARHGEF12 Proteins) (GEF (show ARHGEF2 Proteins)).(

  3. To investigate whether Arl13b has a role in ciliogenesis in mammalian kidney and whether loss of function of Arl13b leads to cystic kidneys in mammals, we generated a mouse model with kidney-specific conditional knockout of Arl13b Deletion of Arl13b in the distal nephron at the perinatal stage led to a cilia biogenesis defect and rapid kidney cyst formation

  4. The authors show that the ciliary G-protein Arl13B, mutated in Joubert syndrome, is the guanine nucleotide exchange factor for Arl3, and its function is conserved in evolution

  5. A new role for Arl13b in actin cytoskeleton remodeling through the interaction with Myh9 (show MYH9 Proteins).

  6. Early neuroepithelial deletion of ciliary Arl13b reversed the apical-basal polarity of radial progenitors & caused aberrant neuronal placement. Arl13b signaling in primary cilia is crucial for initial formation of a polarized radial glial scaffold.

  7. guidance cue receptors essential for interneuronal migration localize to interneuronal primary cilia, but their concentration and dynamics are altered in the absence of Arl13b

  8. By deleting Arl13b in mouse, we induced low-level constitutive GliA function at specific developmental stages and defined a crucial period prior to E10.5 when shifts in the level of GliA cause cells to change their fate

  9. Study shows the cilia protein Arl13b is required for left right axis specification as its absence results in heterotaxia; the defect originates in the node where Cerl2 (show DAND5 Proteins) is not downregulated and asymmetric expression of Nodal is not maintained resulting in symmetric expression of both genes.

  10. The role of Arl13b in ciliogenesis and it's interaction with Smo and Shh proteins.Arl13b regulates the ciliary entry of Smo.

ARL13B Protein Profile

Protein Summary

This gene encodes a member of the ADP-ribosylation factor-like family. The encoded protein is a small GTPase that contains both N-terminal and C-terminal guanine nucleotide-binding motifs. This protein is localized in the cilia and plays a role in cilia formation and in maintenance of cilia. Mutations in this gene are the cause of Joubert syndrome 8. Alternate splicing results in multiple transcript variants.

Gene names and symbols associated with ARL13B

  • ADP-ribosylation factor-like 13B (Arl13b)
  • ADP-ribosylation factor-like 13B (ARL13B)
  • ADP-ribosylation factor-like 13B (arl13b)
  • ADP-ribosylation factor-like 13b (arl13b)
  • A530097K21Rik protein
  • A930014M17Rik protein
  • Arl2l1 protein
  • C530009C10Rik protein
  • chunp6872 protein
  • fc23g07 protein
  • hnn protein
  • JBTS8 protein
  • MGC185757 protein
  • wu:fc23g07 protein
  • zgc:123149 protein

Protein level used designations for ARL13B

ADP-ribosylation factor-like protein 13B , ADP-ribosylation factor-like 2-like 1 , ADP-ribosylation factor-like 13B , ADP-ribosylation factor-like protein 13B-like , ADP-ribosylation factor-like protein 2-like 1 , ARL2-like protein 1 , protein scorpion , scorpion , un-named hi459 , unm hi459

GENE ID SPECIES
304037 Rattus norvegicus
418431 Gallus gallus
460534 Pan troglodytes
487934 Canis lupus familiaris
512781 Bos taurus
694959 Macaca mulatta
100124913 Xenopus (Silurana) tropicalis
100413286 Callithrix jacchus
100456801 Pongo abelii
100467626 Ailuropoda melanoleuca
100600917 Nomascus leucogenys
286784 Danio rerio
200894 Homo sapiens
68146 Mus musculus
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