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Recombinant Monkey CD98 Protein

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DataSheet   

The recombinant monkey CD98 protein is derived from in vitro expression of monkey CD98 gene in E. coli and purified using his-tag affinity column and can be used in multiple applications such as cell culture, ELISA and western blot.

Alternative names for CD98: Cluster of differentiation 98

This product is for Laboratory Research Use Only not for diagnostic and therapeutic purposes or any other purposes.

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Description

Genorise Recombinant Monkey CD98 Protein Summary

Alternative names for CD98: Cluster of differentiation 98

Alternative name for monkey: monkey

Product Specifications

Purity > 97%, by SDSPAGE under reducing conditions and visualized by silver stain.
Endotoxin Level < 0.1 EU per 1 μg of the protein by the LAL method.
Activity na
Source E. coli derived monkey CD98.
Accession # XP_010376652.1
N-Terminal Sequence Analysis Leu
Amino Acid Sequence Leu414-Pro503
Predicted Molecular Mass 10 kDa
SDS-PAGE 10 kDa, reducing conditions

 

Background: 

CD98 is a glycoprotein[1][2] that is a heterodimer composed of SLC3A2 and SLC7A5 that forms the large neutral amino acid transporter (LAT1). LAT1 is a heterodimeric membrane transport protein that preferentially transports branched-chain (valine, leucine, isoleucine) and aromatic (tryptophan, tyrosine) amino acids.[3] LAT is highly expressed in brain capillaries (which form the blood–brain barrier) relative to other tissues.[3] A functional LAT1 transporter is composed of two proteins encoded by two distinct genes: 4F2hc/CD98 heavy subunit protein encoded by the SLC3A2 gene and CD98 light subunit protein encoded by the SLC7A5 gene. LAT1 showed a novel fundamental role to support the protein expression of 4F2hc via a chaperone-like function in chorionic trophoblasts.[4] SLC3A2 is upregulated in osteosarcoma and plays a crucial role in tumor growth.[5] Increased CD98 (4F2hc) expression plays an essential role in tumor aggressiveness and metastasis.[6]

References

  1. Kucharzik T, et al. (2005). Lab. Invest. 85(7): 932–41.
  2. Lemaître G, et al. (2005). Proteomics. 5(14): 3637–45.
  3. Boado RJ, et al. (1999). Proc. Natl. Acad. Sci. U.S.A. 96(21): 12079–84.
  4. Ohgaki R, et al. (2017) Cell. Biol. 37 (11), e00427-16.
  5. Zhu B, et al. (2017)J Oncol. Rep. 37 (5), 2575-2582.
  6. Satoh T, et al. (2017)J Anticancer Res. 37 (2), 631-636.

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