ARSF
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Official Full Name
arylsulfatase F
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Overview
This gene is a member of the sulfatase family, and more specifically, the arylsulfatase subfamily. Members of the subfamily share similarity in sequence and splice sites, and are clustered together on chromosome X, suggesting that they are derived from recent gene duplication events. Sulfatases are essential for the correct composition of bone and cartilage matrix. The activity of this protein, unlike that of arylsulfatase E, is not inhibited by warfarin. Multiple alternatively spliced variants, encoding the same protein, have been identified. -
Synonyms
ARSF; arylsulfatase F; ASF; OTTHUMP00000022857;
- Recombinant Proteins
- Cell & Tissue Lysates
- Human
- E.coli
- E.Coli or Yeast
- HEK293
- In Vitro Cell Free System
- Wheat Germ
- GST
- His
- N/A
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Human | ARSF-3662H | Recombinant Human ARSF, His-tagged | E.Coli or Yeast | His | 590 | |
Human | ARSF-864H | Recombinant Human ARSF protein, GST-tagged | Wheat Germ | GST | ||
Human | ARSF-9900H | Recombinant Human ARSF, GST-tagged | E.coli | GST | 233-590a.a. | |
Human | ARSF-8675HCL | Recombinant Human ARSF 293 Cell Lysate | HEK293 | N/A | ||
Human | ARSF-532H | Recombinant Human ARSF Protein, His-tagged | E.coli | His | His23~Asp300 | |
Human | ARSF-3982H | Recombinant Human ARSF protein, His-tagged | E.coli | His | 233-590 aa | |
Human | ARSF-1017HF | Recombinant Full Length Human ARSF Protein, GST-tagged | In Vitro Cell Free System | GST | 590 amino acids |
- Involved Pathway
- Protein Function
- Interacting Protein
ARSF involved in several pathways and played different roles in them. We selected most pathways ARSF participated on our site, such as Gamma carboxylation, hypusine formation and arylsulfatase activation, Glycosphingolipid metabolism, Metabolism, which may be useful for your reference. Also, other proteins which involved in the same pathway with ARSF were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Gamma carboxylation, hypusine formation and arylsulfatase activation | PROCA;FURINA;WDR85;DPH3;ARSD;GAS6;DNAJC24;ARSF;DPH5 |
Glycosphingolipid metabolism | ARSF;ARSI;ARSH;GLTPD1;ARSK;ARSD;ARSE;NEU3;GLTP |
Metabolism | SCP2B;COX6A1;GSTO2;CYP2Y3;APOF;SIN3B;PPM1LA;CYP2K18;APOBB.1 |
Metabolism of lipids and lipoproteins | ARSJ;ACOT8;SLC27A5;PNPLA8;ACOT9.1;ACOT12;ACSF2;CHKB;BCHE |
Metabolism of proteins | CGB5;YY2;ARSF;SEC22A;PFDN2;MBOAT4;RAB27A;F9A;NSMCE2 |
Post-translational protein modification | SMC5;GALNT13;MAN1A2;ADAMTS5;GALNTL5;B3GNT6;ADAMTSL5;SCMH1;B3GALTL |
Sphingolipid metabolism | CERS2A;ARSK;NEU3.3;NEU3.1;GLTPD1;SPTLC2A;R05D11.9;SGMS1;SUMF2 |
The activation of arylsulfatases | ARSK;SUMF2;ARSF;ARSJ;ARSH;ARSI |
ARSF has several biochemical functions, for example, arylsulfatase activity, metal ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by ARSF itself. We selected most functions ARSF had, and list some proteins which have the same functions with ARSF. You can find most of the proteins on our site.
Function | Related Protein |
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arylsulfatase activity | ARSG;ARSB;ARSA;ARSI;ARSK;ARSJ;ARSF;ARSD;SULF2 |
metal ion binding | PPP1CC;ZSCAN16;ZNHIT3;Car2;PPARG;MGAT1;BCMO1;HIVEP2A;ASXL1 |
ARSF has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ARSF here. Most of them are supplied by our site. Hope this information will be useful for your research of ARSF.
EP300
- Q&As
- Reviews
Q&As (9)
Ask a questionThe ARSF protein may interact with various molecules within the cellular environment. For example, it has been reported to interact with other sulfatases, transporters of sulfate-containing molecules, and certain signaling proteins. These interactions can regulate its activity or contribute to different physiological processes and pathways involving sulfate metabolism.
Therapeutic strategies for ARSF-related disorders such as CDPX2 are still limited. However, some approaches are being explored, including gene therapy, enzyme replacement therapy, and small molecule modulators to restore or enhance ARSF protein function. These strategies hold promise but require further research and development.
The ARSF protein belongs to the sulfatase enzyme family, which includes several other members involved in sulfate metabolism. Each sulfatase enzyme functions on different substrates and has distinct tissue distribution. While the ARSF protein shares similarities with other sulfatases, it has its specific characteristics and plays a unique role in the hydrolysis of certain sulfate esters.
Currently, the ARSF protein is not widely used as a specific diagnostic or prognostic marker for diseases beyond its association with CDPX2. However, as research progresses and our understanding of the ARSF protein expands, it is possible that it may be utilized in the future for diagnostic, prognostic, or even therapeutic purposes in certain diseases or conditions.
While the ARSF protein is primarily known for its involvement in sulfate metabolism, emerging research suggests it may have additional functions. Some studies have suggested that ARSF may play a role in cell adhesion and migration processes, potentially influencing tissue development and repair. Further research is needed to fully understand these additional roles.
Currently, the primary disorder associated with ARSF protein dysregulation is X-linked chondrodysplasia punctata type 2 (CDPX2). This disorder results from mutations in the ARSF gene, leading to deficient or impaired ARSF protein activity. However, there may be other diseases or conditions that involve ARSF dysregulation, and ongoing research continues to investigate its potential involvement in various disorders.
ARSF protein deficiency, specifically CDPX2, can be diagnosed through genetic testing. A blood or saliva sample is usually collected to analyze the DNA and identify mutations in the ARSF gene. Additionally, clinical evaluation and radiographic imaging may be used to confirm the diagnosis.
Currently, there is no specific cure for ARSF protein deficiency or CDPX2. Treatment is usually focused on managing the symptoms and complications associated with the condition. This may include interventions such as physical therapy for skeletal abnormalities, cataract surgery, and supportive care for intellectual disability and other associated issues.
Mutations in the ARSF gene can lead to a deficiency or reduced activity of the ARSF protein. This can result in a condition called chondrodysplasia punctata, specifically X-linked chondrodysplasia punctata type 2 (CDPX2). CDPX2 is characterized by skeletal abnormalities, cataracts, intellectual disability, and other features.
Customer Reviews (3)
Write a reviewIts reliability and effectiveness in generating accurate data make it an indispensable resource, driving scientific exploration and advancing our understanding of protein structure and function
Researchers can rely on the ARSF protein to deliver precise results, enhancing the credibility and efficiency of their experiments.
By incorporating the ARSF protein into electron microscopy studies, researchers gain insights into the intricate three-dimensional architecture of proteins, facilitating a deeper comprehension of their functions and aiding in the development of novel therapeutics.
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