S100 Protein, beta, Recombinant, Human (S100b)

Although histochemical staining of the S100 protein family has been used for many years in the diagnosis of malignant melanoma, recent studies suggest one of the proteins comprising the S100 family, S100B, has particular utility in many aspects of the clinical management of malignant melanoma. This protein has been shown to be of use in staging malignant melanoma, in establishing prognosis, in evaluating treatment success and in predicting relapse. S100B is an independent prognostic factor and pretreatment circulating S100B concentrations predict duration of survival in melanoma patients. Survival is significantly longer in melanoma patients with normal S100B levels compared to those with elevated levels.\n\nSingle, non-glycosylated polypeptide with containing 91aa (2-92) with an N-terminal hexahistidine tag.\n\nRecombinant protein corresponding to full length human S1000b expressed in E. coli.\n\nAmino Acid Sequence:\nMGSSHHHHHH SSGLVPRGSH MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE.\n\nApplications: \nSuitable for use in ELISA, Western Blot and Inhibition Studies. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, aliquot and store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

S0052-11M

Size

2ug

Applications

ELISA, WB

Form

Supplied as a liquid in 20mM Tris-HCl, pH 8, 50% gylcerol.

Purity

(same/more than) 90% by RP-HPLC, or SDS-PAGE. Chromatographically purified.

References

1. Senmarker S, et al., Perfusion 2004 Nov;19(6):337-43 2. Schaf DV, et al., Parkinsonism Relat Disord 2005 Jan;11(1):39-43 3. Controversial significance of early S100B levels after cardiac surgery. Jonsson H, Johnsson P, Alling C, BMC Neurol 2004 Dec 16;4(1):24 4. Redox modifications of the C-terminal cysteine residue cause structural changes in S100A1 and S100B proteins. Zhukova L, Zhukov I, Wyslouch-Cieszynska A, Biochim Biophys Acta 2004 Dec 6;1742(1-3):191-201 5. S100B-stimulated NO production by BV-2 microglia is independent of RAGE transducing activity but dependent on RAGE extracellular domain. Adami C, Bianchi R, Donato R, Biochim Biophys Acta 2004 Dec 6;1742(1-3):169-77 6. S100B protein is released by in vitro trauma and reduces delayed neuronal injury. Willoughby KA, Kleindienst A, Chen T, J Neurochem 2004 Dec;91(6):1284-91.