RABBIT ANTI HUMAN CD98 LIGHT CHAIN

GWB-61A3F5

Polyclonal IgGSpecies Cross Reactivity: Based on sequence similarity is expected to react with:Mouse RatN. B. Antibody reactivity and working conditions may vary between species.

Recognises an internal domain of the Human CD98 light chain (CD98LC) also known as the 4F2 light chain or LAT-1. CD98LC is a 55kDa multi-pass membrane protein which forms a heterodimer with the CD98 heavy chain to allow transport of large branched chain neutral amino acids into the cell. This transport system leads to the uptake of seven amino acids including isoleucine phenylalanine and methionine. The expression levels of CD98LC are upregulated in a wide spectrum of primary human cancers. Changes in amino acid transporter expression are thought to be an early change in oncogenesis as they impart growth and survival advantages. Recommended Secondary Antibodies: Sheep Anti Rabbit IgGGoat Anti Rabbit IgG (Fc)Goat Anti Rabbit IgG (H/L)

Located to the plasma membrane by SLC3A2/4F2hc. Localized to the apical membrane of placental syncytiophoblastic cells. Expressed in both luminal and abluminal membranes of brain capillary endothelial cells By similarity. Ref. 10Ref. 11Ref. 13Ref. 15Ref. 21Ref. 18Tissue specificityExpressed abundantly in adult lung liver brain skeletal muscle placenta bone marrow testis resting lymphocytes and monocytes and in fetal liver. Weaker expression in thymus cornea retina peripheral leukocytes spleen kidney colon and lymph node. During gestation expression in the placenta was significantly stronger at full-term than at the mid-trimester stage. Also expressed in all human tumor cell lines tested and in the astrocytic process of primary astrocytic gliomas. Expressed in retinal endothelial cells and in the intestinal epithelial cell line Caco-2. Ref. 2Ref. 4Ref. 11Ref. 13Ref. 21Ref. 18Ref. 3Ref. 7Ref. 16Induction: Expression induced in quiescent peripheral blood lymphocytes after treatment with PMA (phorbol myristate acetate)/PHA (phytohemagglutinin). Expression and the uptake of leucine is stimulated in mononuclear cytotrophoblast-like choriocarcinoma cells by combined treatment with PMA and calcium ionophore. Ref. 13Ref. 7Miscellaneous: The uptake of leucine tyrosine and tryptophan is inhibited by the different iodothyronines in particular T3. Leucine transport is also inhibited by small zwitterionic amino acids (i. e. glycine alanine serine threonine and cysteine) and by glutamine and asparginine. The uptake of T3 is almost completely blocked by coincubation with leucine tryptophan tyrosine and phenylalanine or 2-amino-bicyclo-(2 2 1)-heptane-2-carboxylate (BCH). Methionine uptake was inhibited by the L-system substrates L-leucine BCH L-cysteine and by the MeHg-L-cysteine complex and structurally related S-ethyl-L-cysteine. MeHg-L-cysteine uptake is inhibited by L-methionine L-leucine BCH and S-ethyl-L-cysteine. L-leucine uptake was inhibited by L-CNSO. Tyrosine uptake in fibroblasts was inhibited by D-methionine and methyl-aminoisobutyric acid (MeAIB). Sequence similaritiesBelongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2. A. 3. 8) family. [View classification]Biophysicochemical properties Kinetic parameters:KM=7. 9 & micro; M for T4 (in the presence of choline chloride) Ref. 9Ref. 12Ref. 14Ref. 15Ref. 23KM=0. 8 & micro; M for T3 (in the presence of choline chloride)KM=12. 5 & micro; M for reverse triiodothyronine (rT3) (in the presence of choline chloride)KM=7. 9 & micro; M for 3 3\' -diiodothyronine (in the presence of choline chloride)KM=46 & micro; M for leucine (in the presence of choline chloride)KM=19 & micro; M for tryptophan (in the presence of choline chloride)KM=32 & micro; M for L-leucineKM=10 mM for L-alanineKM=2. 2 mM for L-glutamineKM=35 & micro; M for L-histidineKM=740 & micro; M for L-phenylalanineKM=98 & micro; M for MeHg-L-cysteineKM=99 & micro; M for methionineKM=55. 2 & micro; M for phenylalanine (in T24 human bladder carcinoma cells)KM=60. 4 & micro; M for tyrosine (in T24 human bladder carcinoma cells)KM=16. 4 & micro; M for tyrosine (in human fibroblasts)KM=138 & micro; M for Dopa (in T24 human bladder carcinoma cells)KM=96. 5 & micro; M for 3-O-methyldopa (in T24 human bladder carcinoma cells)KM=153 & micro; M for alpha-methyltyrosine (in T24 human bladder carcinoma cells)KM=216 & micro; M for alpha-methyldopa (in T24 human bladder carcinoma cells)KM=191 & micro; M for gabapentin (in T24 human bladder carcinoma cells)KM=7. 3 & micro; M for triiodothyronine (in T24 human bladder carcinoma cells)KM=162 & micro; M for thyroxine (in T24 human bladder carcinoma cells)KM=75. 3 & micro; M for melphanan (in T24 human bladder carcinoma cells)KM=156 & micro; M for BCH (in T24 human bladder carcinoma cells) 1. Favaloro E. J. et al. (1987) Characterisation of monoclonal antibodies to the human myeloid-specific antigen \' gp67\' (CD-33). Dis Markers. 5: 215-225. 2. Favaloro E. J. et al. (1988) Further characterisation of myeloid antigens (\' gp160 95\' \' gp150\' and \' gp67\' ): Investigation of epitopic heterogeneity and non-haemopoietic distribution using panels of monoclonal antibodies belonging to CD-11b CD-13 and CD33. Br. J. Haematol. 69: 163-171. [1] \" Isolation of a cDNA encoding CD33 a differentiation antigen of myeloid progenitor cells. \" Simmons D. Seed B. J. Immunol. 141:2797-2800(1988) [PubMed: 3139766] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] VARIANT GLY-69. Tissue: Premonocytic lymphoma. [2] \" Genomic organization of the siglec gene locus on chromosome 19q13. 4 and cloning of two new siglec pseudogenes. \" Yousef G. M. Ordon M. H. Foussias G. Diamandis E. P. Gene 286:259-270(2002) [PubMed: 11943481] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. [3] \" The status quality and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). \" The MGC Project TeamGenome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] VARIANT GLY-69. Tissue: Leukocyte. [4] \" Characterization of CD33 as a new member of the sialoadhesin family of cellular interaction molecules. \" Freeman S. D. Kelm S. Barber E. K. Crocker P. R. Blood 85:2005-2012(1995) [PubMed: 7718872] [Abstract]Cited for: SIALIC ACID-BINDING. [5] \" The sialoadhesin CD33 is a myeloid-specific inhibitory receptor. \" Ulyanova T. Blasioli J. Woodford-Thomas T. A. Thomas M. L. Eur. J. Immunol. 29:3440-3449(1999) [PubMed: 10556798] [Abstract]Cited for: FUNCTION PHOSPHORYLATION AT TYR-340 AND TYR-358 MUTAGENESIS OF TYR-358 INTERACTION WITH PTPN6. [6] \" The myeloid-specific sialic acid-binding receptor CD33 associates with the protein-tyrosine phosphatases SHP-1 and SHP-2. \" Taylor V. C. Buckley C. D. Douglas M. Cody A. J. Simmons D. L. Freeman S. D. J. Biol. Chem. 274:11505-11512(1999) [PubMed: 10206955] [Abstract]Cited for: PHOSPHORYLATION AT TYR-340 AND TYR-358 INTERACTION WITH PTPN6 AND PTPN11 MUTAGENESIS OF TYR-340. [7] \" Surface expression and function of p75/AIRM-1 or CD33 in acute myeloid leukemias: engagement of CD33 induces apoptosis of leukemic cells. \" Vitale C. Romagnani C. Puccetti A. Olive D. Costello R. Chiossone L. Pitto A. Bacigalupo A. Moretta L. Mingari M. C. Proc. Natl. Acad. Sci. U. S. A. 98:5764-5769(2001) [PubMed: 11320212] [Abstract]Cited for: FUNCTION.