Recombinant human PMEL Protein with C-terminal Human Fc tag
Figure 1. Human PMEL Protein, hFc Tag on SDS-PAGE under reducing condition.
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Amount : | 50 µg |
Purification : | The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. |
Content : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8% trehalose is added as protectants before lyophilization. |
Storage condition : | Store at -80°C for 12 months (Avoid repeated freezing and thawing) |
Alternative Name : | D12S53E, gp100, ME20, ME20-M, ME20M, P1, P100, PMEL17, SI, SIL, SILV |
Expression Host : HEK293
The protein has a predicted molecular mass of 46.2 kDa after removal of the signal peptide.The apparent molecular mass of PMEL-hFc is approximately 130-250 kDa due to glycosylation.
This gene encodes a melanocyte-specific type I transmembrane glycoprotein. The encoded protein is enriched in melanosomes, which are the melanin-producing organelles in melanocytes, and plays an essential role in the structural organization of premelanosomes. This protein is involved in generating internal matrix fibers that define the transition from Stage I to Stage II melanosomes. This protein undergoes a complex pattern of prosttranslational processing and modification that is essential to the proper functioning of the protein. A secreted form of this protein that is released by proteolytic ectodomain shedding may be used as a melanoma-specific serum marker. Alternate splicing results in multiple transcript variants.
The protein has a predicted molecular mass of 46.2 kDa after removal of the signal peptide.The apparent molecular mass of PMEL-hFc is approximately 130-250 kDa due to glycosylation.
This gene encodes a melanocyte-specific type I transmembrane glycoprotein. The encoded protein is enriched in melanosomes, which are the melanin-producing organelles in melanocytes, and plays an essential role in the structural organization of premelanosomes. This protein is involved in generating internal matrix fibers that define the transition from Stage I to Stage II melanosomes. This protein undergoes a complex pattern of prosttranslational processing and modification that is essential to the proper functioning of the protein. A secreted form of this protein that is released by proteolytic ectodomain shedding may be used as a melanoma-specific serum marker. Alternate splicing results in multiple transcript variants.
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