PDF《Ramp4/4-2 (G-16): sc-85115》

SANTA CRUZ BIOTECHNOLOGY, INC.

Ramp4/4-2 (G-16): sc-85115 Santa Cruz Biotechnology, Inc. 1.800.457.3801 831.457.3800 fax 831.457.3801 Europe +00800

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4503 0 www.scbt.com BACKGROUND Newly synthesized proteins emerging through the endoplasmic reticulum (ER) membrane enter a unique environment for folding and assembly by associated proteins. RAMP4 (ribosome-attached membrane protein 4), also designated SERP1 (stress-associated endoplasmic reticulum protein family member 1) and RAMP4-2 (ribosome-associated membrane protein 4-2), also known as SERP2 (stress-associated endoplasmic reticulum protein family member 2), are sin- gle-pass type IV membrane proteins that localize to the ER and belong to the RAMP4 family. RAMP4 and RAMP4-2 may interact with target proteins during translocation into the lumen of the ER and protect unfolded target proteins against degradation during ER stress. After termination of ER stress, RAMP4 and RAMP4-2 are involved in facilitating glycosylation of target proteins. RAMP4 consists of

66 amino acids and is encoded by a gene located on human chromosome 3, whereas RAMP4-2 is encoded by a gene located on human chromosome

13 and is composed of

61 amino acids. REFERENCES 1. Wei, J. and Hendershot, L.M. 1996. Protein folding and assembly in the endoplasmic reticulum. EXS 77: 41-55. 2. Trombetta, E.S. and Helenius, A. 1998. Lectins as chaperones in glycopro- tein folding. Curr. Opin. Struct. Biol. 8: 587-592. 3. Schr?der, K., Martoglio, B., Hofmann, M., H?lscher, C., Hartmann, E., Prehn, S., Rapoport, T.A. and Dobberstein, B. 1999. Control of glycosylation of MHC class II-associated invariant chain by translocon-associated RAMP4. EMBO J. 18: 4804-4815. 4. Yamaguchi, A., Hori, O., Stern, D.M., Hartmann, E., Ogawa, S. and Tohyama, M. 1999. Stress-associated endoplasmic reticulum protein

1 (SERP1)/ ribosome-associated membrane protein

4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation. J. Cell Biol. 147: 1195-1204. 5. Parodi, A.J. 2000. Protein glucosylation and its role in protein folding. Annu. Rev. Biochem. 69: 69-93. 6. High, S., Lecomte, F.J., Russell, S.J., Abell, B.M. and Oliver, J.D. 2000. Glycoprotein folding in the endoplasmic reticulum: a tale of three chaper- ones? FEBS Lett. 476: 38-41. 7. Hori, O., Miyazaki, M., Tamatani, T., Ozawa, K., Takano, K., Okabe, M., Ikawa, M., Hartmann, E., Mai, P., Stern, D.M., Kitao, Y. and Ogawa, S. 2006. Deletion of SERP1/RAMP4, a component of the endoplasmic reticulum (ER) translocation sites, leads to ER stress. Mol. Cell. Biol. 26: 4257-4267. 8. Shen, Y., Wilder-Smith, E., Yu, E., Ng, Y.K., Ling, E.A., Spence, I. and Wong, M.C. 2007. A novel methodology to probe endothelial differential gene expression profile reveals novel genes. Endothelium 14: 303-314. 9. Favaloro, V., Spasic, M., Schwappach, B. and Dobberstein, B. 2008. Distinct targeting pathways for the membrane insertion of tail-anchored (TA) pro- teins. J. Cell Sci. 121: 1832-1840. CHROMOSOMAL LOCATION Genetic locus: SERP1 (human) mapping to 3q25.1, SERP2 (human) mapping to 13q14.11;

Serp1 (mouse) mapping to

3 D, Serp2 (mouse) mapping to

14 D3. SOURCE Ramp4/4-2 (G-16) is an affinity purified rabbit polyclonal antibody raised against a peptide mapping within an internal region of Ramp4-2 of human origin. PRODUCT Each vial contains

100 ?g IgG in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin. Blocking peptide available for competition studies, sc-85115 P, (100 ?g peptide in 0.5 ml PBS containing < 0.1% sodium azide and 0.2% BSA). APPLICATIONS Ramp4/4-2 (G-16) is recommended for detection of Ramp4-2 and Ramp4 of mouse, rat and human origin by Western Blotting (starting dilution 1:200, dilution range 1:100-1:1000), immunoprecipitation [1-2 ?g per 100-500 ?g of total protein (1 ml of cell lysate)], immunofluorescence (starting dilution 1:50, dilution range 1:50-1:500) and solid phase ELISA (starting dilution 1:30, dilu- tion range 1:30-1:3000);