Recombinant Human CFHR1 (C-6His)
- Cat. No.：EPT123
- Price：USD $ 3,780.00
- Clicks：991
Product Detail
Basic Information
| Size | 50ug |
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| Expression Host | Human Cells |
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| Tag | C-6His |
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Physical Properties
| Molecular Weight | 36.78 KDa |
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| Apparent Molecular Weight | 39-43 KDa, reducing conditions |
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| Form | Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, 2mM EDTA, pH 7.4. |
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| Purity | Greater than 95% as determined by reducing SDS-PAGE. |
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Activity & Endotoxin
| Endotoxin Level | Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test. |
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Storage & Shipping
| Reconstitution | Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
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| Storage | Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at < -20°C for 3 months. |
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| Shipping Condition | The product is shipped at ambient temperature.
Upon receipt, store it immediately at the temperature listed below. |
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Detailed Description
| Background | Complement Factor H-Related 1 (CFHR1) is a 43 kDa secreted member of the factor H family of glycoproteins. The human Complement Factor H protein family consists of the complement and immune regulators factor H, the factor H-like protein 1 (FHL-1) and five factor H-related proteins (CFHR-1 to -5). Members of the H-related protein family are exclusively composed of individually folded protein domains, termed short consensus repeats (SCRs) or complement control modules. FHR1 is produced by hepatocytes and circulates as two differentially glycosylated isoforms (37 kDa and 43 kDa). Mature human FHR1 is 312 amino acids in length. It contains five, approximately 60 aa SCRs that basically constitute the entire molecule. FHR1 may play a role in complement regulation, lipid metabolism and lipoprotein complexes that bind PMNs to LPS. |
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