Recombinant Human ARSL Protein, Myc/DDK-tagged, C13 and N15-labeled
Cat.No. : | ARSL-441H |
Product Overview : | ARSE MS Standard C13 and N15-labeled recombinant protein (NP_000038) with a C-terminal MYC/DDK tag, was expressed in HEK293 cells. |
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Description : | Arylsulfatase E is a member of the sulfatase family. It is glycosylated postranslationally and localized to the golgi apparatus. Sulfatases are essential for the correct composition of bone and cartilage matrix. X-linked chondrodysplasia punctata, a disease characterized by abnormalities in cartilage and bone development, has been linked to mutations in this gene. Alternative splicing results in multiple transcript variants. A pseudogene related to this gene is located on the Y chromosome. |
Source : | HEK293 |
Species : | Human |
Tag : | Myc&DDK |
Molecular Mass : | 65.7 kDa |
AA Sequence : | MLHLHHSCLCFRSWLPAMLAVLLSL APSASSDISASRPNILLLMADDLGI GDVGCYGNNTMRTPNIDRLAEDGVK LTQHISAASLCTPSRAAFLTGRYPV RSGMVSSIGYRVLQWTGASGGLPTN ETTFAKILKEKGYATGLIGKWHLGL NCESASDHCHHPLHHGFDHFYGMPF SLMGDCARWELSEKRVNLEQKLNFL FQVLALVALTLVAGKLTHLIPVSWM PVIWSALSAVLLLASSYFVGALIVH ADCFLMRNHTITEQPMCFQRTTPLI LQEVASFLKRNKHGPFLLFVSFLHV HIPLITMENFLGKSLHGLYGDNVEE MDWMVGRILDTLDVEGLSNSTLIYF TSDHGGSLENQLGNTQYGGWNGIYK GGKGMGGWEGGIRVPGIFRWPGVLP AGRVIGEPTSLMDVFPTVVRLAGGE VPQDRVIDGQDLLPLLLGTAQHSDH EFLMHYCERFLHAARWHQRDRGTMW KVHFVTPVFQPEGAGACYGRKVCPC FGEKVVHHDPPLLFDLSRDPSETHI LTPASEPVFYQVMERVQQAVWEHQR TLSPVPLQLDRLGNIWRPWLQPCCG PFPLCWCLREDDPQTRTRPLEQKLI SEEDLAANDILDYKDDDDKV |
Purity : | > 80% as determined by SDS-PAGE and Coomassie blue staining |
Stability : | Stable for 3 months from receipt of products under proper storage and handling conditions. |
Storage : | Store at -80 centigrade. Avoid repeated freeze-thaw cycles. |
Concentration : | 50 μg/mL as determined by BCA |
Storage Buffer : | 100 mM glycine, 25 mM Tris-HCl, pH 7.3. |
Gene Name : | ARSL arylsulfatase L [ Homo sapiens (human) ] |
Official Symbol : | ARSL |
Synonyms : | ARSL; arylsulfatase L; ASE; ARSE; CDPX; CDPX1; CDPXR; arylsulfatase L; arylsulfatase E (chondrodysplasia punctata 1); EC 3.1.6.1 |
Gene ID : | 415 |
mRNA Refseq : | NM_000047 |
Protein Refseq : | NP_000038 |
MIM : | 300180 |
UniProt ID : | P51690 |
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Customer Reviews (3)
Write a reviewIts versatility and consistent performance make it an indispensable tool for a wide range of research applications.
Whether it's protein quantification, structural analysis, or Western Blotting, the ARSL protein has consistently delivered exceptional results, earning my highest recommendation.
The ARSL protein has proven invaluable in protein electron microscopy structure analysis, allowing for detailed investigations and providing critical insights.
Q&As (11)
Ask a questionCurrently, there is no documented evidence linking ARSL gene mutations to developmental abnormalities. However, since the ARSL protein is involved in important metabolic processes, it is possible that severe disruptions in its function could have developmental consequences.
While no direct links between ARSL gene variations and drug metabolism or response have been reported, disturbances in sulfated compound metabolism, which ARSL participates in, can indirectly influence drug pharmacokinetics and efficacy. Further research is needed to fully understand these relationships.
The ARSL protein is widely expressed in various tissues, including the liver, kidney, brain, and intestines, among others. Its expression pattern reflects its involvement in the metabolism of sulfated compounds throughout the body.
Currently, there are no known diseases specifically associated with mutations in the ARSL gene. However, dysregulation or deficiency of ARSL activity may contribute to certain disorders that involve impaired sulfated compound metabolism.
The expression of the ARSL protein can vary depending on the tissue type, developmental stage, and specific physiological conditions. Research suggests that factors such as inflammation and cellular stress can influence ARSL expression levels to regulate sulfated compound metabolism.
While currently there is no known direct link between ARSL dysfunction and neurodegenerative disorders, disturbances in sulfated compound metabolism have been implicated in some neurodegenerative diseases. Further research is necessary to determine if ARSL dysfunction contributes to these conditions.
The ARSL protein contains specific targeting sequences that facilitate its transport to the lysosomes, where it carries out its enzymatic activity. Trafficking of ARSL from the endoplasmic reticulum to the lysosomes involves interactions with various intracellular transport machinery.
While the therapeutic targeting of the ARSL protein itself is not currently explored extensively, the manipulation of its activity or related pathways may hold potential for certain diseases involving abnormal sulfated compound metabolism. Further research is needed to determine the therapeutic implications of ARSL modulation.
Yes, the ARSL protein is conserved across multiple organisms, including mammals, birds, fish, and certain invertebrates. This suggests its significance in sulfated compound metabolism is evolutionarily conserved.
The ARSL protein is not directly associated with lysosomal storage disorders. However, disturbances in lysosomal function, which is involved in the breakdown of sulfated compounds, can impact ARSL-mediated pathways, potentially contributing to the pathogenesis of lysosomal storage disorders.
Currently, specific modulators or inhibitors of the ARSL protein have not been reported. However, it is possible that compounds or molecules affecting sulfated compound metabolism or lysosomal function could indirectly alter the activity of ARSL.
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