Recombinant Human Secretoglobin Family 1D Member 1
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| Amount : | 10 µg |
| Purification : | as determined by densitometric image analysis is greater than 95%. |
| Content : | SCGB1D1 filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5. |
| Storage condition : | Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. |
| AA sequence : | MKHHHHHHAS VVCQALGSEI TGFLLAGKPV FKFQLAKFKA PLEAVAAKME VKKCVDTMAY EKRVLITKTL GKIAEKCDR. |
| Alternative Name : | Secretoglobin family 1D member 1, Lipophilin-A, SCGB1D1, LIPHA, LPNA, LIPA, LPHA. |
Source : Escherichia Coli.
SCGB1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 22-90) containing 79 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 8.8kDa (calculated).
Secretoglobin Family 1D, Member 1 (SCGB1D1) belongs to the lipophilin subfamily, part of the uteroglobin superfamily, and is an ortholog of prostatein (which is the major secretory glycoprotein of the rat ventral prostate gland). SCGB1D1 binds androgens and other steroids. In addition SCGB1D1 binds chemotherapeutic drugs during the prostate cancer treatment. Steroid hormones regulate the SCGB1D1 transcription. SCGB1D1 is secreted into extracellular space. SCGB1D1 gene product represents one component of a heterodimeric molecule found in human tears whose elution profile is consistent with prostatein (which is a tetrameric molecule comprised of 3 peptide components in heterodimers).
It is recommended to add 200µl deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SCGB1D1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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